From owner-proteins@net.bio.net Thu Jul 01 02:39:00 1999 Path: biosci!agate!newsfeed.berkeley.edu!dispose.news.demon.net!demon!feed1.news.rcn.net!rcn!nntp.abs.net!newshub2.home.com!newshub1.home.com!news.home.com!news.rdc1.tn.home.com.POSTED!not-for-mail Message-ID: <377B441E.2A174BAE@uab.edu> From: Peter Prevelige Reply-To: prevelig@uab.edu Organization: Dept. of Microbiology, UAB X-Mailer: Mozilla 4.5 C-AtHome0405(Macintosh; U; PPC) X-Accept-Language: en MIME-Version: 1.0 Newsgroups: bionet.molbio.proteins Subject: Re: CD alpha helix percentage References: <377AADD9.94EAB33@uab.edu> Content-Type: multipart/mixed; boundary="------------DAE003A57498BFA92BBC3D31" Date: Thu, 01 Jul 1999 10:34:06 GMT NNTP-Posting-Host: 24.2.24.8 X-Complaints-To: abuse@home.net X-Trace: news.rdc1.tn.home.com 930825246 24.2.24.8 (Thu, 01 Jul 1999 03:34:06 PDT) NNTP-Posting-Date: Thu, 01 Jul 1999 03:34:06 PDT Lines: 117 This is a multi-part message in MIME format. --------------DAE003A57498BFA92BBC3D31 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit To follow up, on Dr. Gussakovsky's point: the contributing factor is far UV CD is the peptide bond. Therefore, one mole of a 20 amino acid peptide will produce twice the raw CD signal that one mole of a decapeptide will produce, even if they are both in fully helical conformations. Likewise two moles of a fully helical decapeptide will produce the same amount of signal as one mole of a helical 20 amino acid fragment. Therefore, you need to determine the concentration of amino-acids, and normalize to this number. ie: 2 moles * 10 amino acids/peptide = 20 moles amino acids 1 mole * 20 amino acids/peptide = 20 moles amino acids you can obtain this number by knowing the molar concentration of the protein and the number of amino acids/molecular, or alternatively by knowing the weight concentration and the average weight of the amino acids (which is generally approximately 110). Realize that for fitting CD spectra, the determination of the concentration is very important, because you are fitting based on the magnitude of the spectra as much as their shape. In fact, if you use some of the simpler schemes for calculating helix, they are exclusively magnitude based. Peter "Dr. Eugene Gussakovsky 03-9683409 vh" wrote: > > On Wed, 30 Jun 1999, Peter Prevelige wrote: > > > This is a multi-part message in MIME format. > > --------------5D372F1FB607262920564997 > > Content-Type: text/plain; charset=us-ascii > > Content-Transfer-Encoding: 7bit > > > > Far UV CD spectra should be calculated in terms of deg cm2 dmol/ AMINO > > ACID. In this manner, tey are independent of the protein concentration, > > as well as the molecular weight of the protein. Therefore, there is no > > concentration dependent change in helicity, unless there is molecular > > association going on. > > > > > > > > Young Chai wrote: > > > > > > Could you tell me that there are any differences of the percentage of > > > alpha helix from CD spectra with different protein concentration? > > > I appreciate kind answers. > > > > > > Young Chai > > --------------5D372F1FB607262920564997 > > Content-Type: text/x-vcard; charset=us-ascii; > > name="prevelig.vcf" > > Content-Transfer-Encoding: 7bit > > Content-Description: Card for Peter Prevelige > > Content-Disposition: attachment; > > filename="prevelig.vcf" > > > > begin:vcard > > n:Prevelige;Peter > > tel;fax:205 975-5479 > > x-mozilla-html:FALSE > > url:http://www.microbio.uab.edu/faculty/Prevelige/prevelige-p.htm > > org:Univ. of Alabama at Birmingham;Microbiology > > version:2.1 > > email;internet:prevelig@uab.edu > > title:Associate Professor > > adr;quoted-printable:;;BBRB 416/6=0D=0A845 19th St. South;Birmingham;AL;35294;USA > > x-mozilla-cpt:;3 > > fn:Peter Prevelige > > end:vcard > > > > --------------5D372F1FB607262920564997-- > > > > > > > But a CD spectrum intensity does depend on the protein concentration. So > to calculate a secondary structure from CD, the protein concentration is > necessary while the sendary structure itself is concetration-independent > as Prof.Prevelige noted correctly. > > Best wishes. > Dr.Eugene Gussakovsky > > --- --------------DAE003A57498BFA92BBC3D31 Content-Type: text/x-vcard; charset=us-ascii; name="prevelig.vcf" Content-Transfer-Encoding: 7bit Content-Description: Card for Peter Prevelige Content-Disposition: attachment; filename="prevelig.vcf" begin:vcard n:Prevelige;Peter tel;fax:205 975-5479 x-mozilla-html:FALSE url:http://www.microbio.uab.edu/faculty/Prevelige/prevelige-p.htm org:Univ. of Alabama at Birmingham;Microbiology version:2.1 email;internet:prevelig@uab.edu title:Associate Professor adr;quoted-printable:;;BBRB 416/6=0D=0A845 19th St. South;Birmingham;AL;35294;USA x-mozilla-cpt:;3 fn:Peter Prevelige end:vcard --------------DAE003A57498BFA92BBC3D31-- From owner-proteins@net.bio.net Thu Jul 01 07:19:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!easynet-fr!ciril.fr!univ-lille1.fr!not-for-mail From: "Philippe CHAVATTE" Newsgroups: bionet.molbio.proteins Subject: Proteins comparison Date: Thu, 1 Jul 1999 17:10:23 +0200 Organization: Universite des Sciences et Technologies de LILLE, France Lines: 23 Message-ID: <7lg0i8$s4f$1@netserv.univ-lille1.fr> NNTP-Posting-Host: icp16.univ-lille2.fr X-Newsreader: Microsoft Outlook Express 4.72.2106.4 X-MimeOLE: Produced By Microsoft MimeOLE V4.72.2106.4 What is the best methodology to compare two protein 3D structures (pdb format) ? What criteria permit to affirm their similarity ? Many thanks for your help. Philippe -- ----------------- Philippe CHAVATTE Institut de Chimie Pharmaceutique Albert Lespagnol BP 83 59006 LILLE CEDEX FRANCE E-Mail : pchavatt@phare.univ-lille2.fr From owner-proteins@net.bio.net Thu Jul 01 12:11:00 1999 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!feed1.news.rcn.net!rcn!not-for-mail From: Aptagen Researcher Newsgroups: bionet.molbio.proteins Subject: Denaturing endogenous alkaline phosphatase Date: Thu, 01 Jul 1999 16:04:03 -0400 Lines: 7 Message-ID: <377BC9B2.69844525@Aptagen.com> Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Trace: AWjdD2C2PQDh5kw0r018Jo3IGlef0juPGF7bUk5tpgU= X-Complaints-To: abuse@rcn.com NNTP-Posting-Date: 1 Jul 1999 20:05:46 GMT X-Corel-MessageType: EMail X-Mailer: Mozilla 4.04 [en] (Win95; U) I am doing a spot blot on pichia extracts. I have an abnormally high background, and I believe it is due to endogenous alkaline phosphatase. Does anybody have any suggestions on how I can denature endogenous alkaline phosphatase do reduce the background? Mike From owner-proteins@net.bio.net Thu Jul 01 16:02:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!paloalto-snf1.gtei.net!news.gtei.net!enews.sgi.com!lll-winken.llnl.gov!not-for-mail From: Mark Knapp Newsgroups: bionet.molbio.proteins Subject: Wanted: Protein Chem/molecular Biol. Date: Thu, 01 Jul 1999 16:58:01 -0700 Organization: Lawrence Livermore National Laboratory Lines: 83 Message-ID: <377C0088.155FCB31@llnl.gov> NNTP-Posting-Host: antigone.llnl.gov Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Trace: lll-winken.llnl.gov 930873404 20430 128.115.17.115 (1 Jul 1999 23:56:44 GMT) X-Complaints-To: abuse@lll-winken.llnl.gov NNTP-Posting-Date: 1 Jul 1999 23:56:44 GMT X-Mailer: Mozilla 4.5 [en] (WinNT; U) X-Accept-Language: en The Macromolecular Crystallography Group at Lawrence Livermore National Laboratory has an immediate opening for a Protein Chemist/Molecular Biologist. Pleas see our website for further details: http://www-structure.llnl.gov/Jobapps/openjobs.html ]BS 6273 - Postdoctoral Protein Chemist or Molecular Biologist A postdoctoral position for a Protein Chemist or Molecular Biologist is available immediately in the Macromolecular Crystallography group in the Biology and Biotechnology Research Program on a University of California Campus-Laboratory-Collaboration (CLC) project on the structural genomics of Pyrobaculum Aerophilum (PA). Nature and Scope of Position: The individual will work as a member of a research team and be fully responsible for work on genes from the extremophile Pyrobaculum Aerophilum as a member of a pilot study on structural genomics initiated by Prof. Eisenberg at UCLA. The challenge will be to integrate molecular biology, biochemistry and crystallography. We have specific need for cloning, mutagenesis, expression, and purification skills. An interest in crystallography is desirable and some knowledge of crystallography is preferred but not necessary. A qualified applicant should work independently while cloning and over expressing proteins of interest and should be able to devise purification protocols. The current focus of related research efforts in the macromolecular crystallography group includes, DNA repair enzymes, bacterial neurotoxins, and lipoproteins. Essential Duties: Oversee day-to-day operation of protein expression, purification and analysis Clone and amplify PA genes of interest from C-DNA libraries Over express and purify PA proteins Maintain and expand LLNL PA web pages Help coworkers and other investigators with expression and purification Assist in the writing of manuscripts MARGINAL DUTIES: Help supervise summer students and visiting faculty Perform routine laboratory safety checks Manage waste generated in the laboratory Essential Skills, Knowledge, and Abilities: Ph.D in the biochemistry, genetics, molecular biology or related fields. Experience in gene expression and protein purification Should feel comfortable working with instrumentation and personal computers Must be capable of working with minimal supervision and making independent decisions Desired Skills, Knowledge, and Abilities: Previous experience with protein crystallization TO APPLY, CONTACT: Bernhard Rupp, Biology and Biotechnology Research Program, L-452, P.O. Box 808, Lawrence Livermore National Laboratory, Livermore, CA 94551, br@llnbl.gov, http://www-structure.llnl.gov Please refer to the posting at our website http://www-structure.llnl.gov/Jobapps/openjobs.html -- ********************************************************************* Ducks usually lie. -- DM Pinkwater ********************************************************************* Mark Knapp Lawrence Livermore National Laboratory Macromolecular Crystallography Group http://www-structure.llnl.gov Mail Stop L-452 Office: 925-422-5793 7000 East Avenue, PO Box 808 Fax : 925-422-2282 Livermore, CA 94550 email: knapp14@llnl.gov From owner-proteins@net.bio.net Sun Jul 04 10:55:00 1999 Newsgroups: bionet.molbio.proteins Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!dispose.news.demon.net!demon!nntp.news.xara.net!xara.net!server6.netnews.ja.net!leeds.ac.uk!news From: bmbjmm@bmb.leeds.ac.uk (Jeremy Murray) Subject: Re: Proteins comparison X-Accept-Language: en Message-ID: <377FA6CF.BA24BF64@bmb.leeds.ac.uk> NNTP-Posting-Host: bmbpc232.leeds.ac.uk X-Mailer: Mozilla 4.5 [en] (Win95; I) Content-Type: text/plain; charset=us-ascii Organization: University of Leeds MIME-Version: 1.0 Date: Sun, 4 Jul 1999 19:20:10 +0100 (BST) References: <7lg0i8$s4f$1@netserv.univ-lille1.fr> To: Philippe CHAVATTE Content-Transfer-Encoding: 7bit Lines: 33 wotcha Philippe u could try lsqman http://alpha2.bmc.uu.se/~gerard/manuals/lsqman_man.html and note the root mean square distances for alpha carbons for putative equivalent residues but there are a bunch of other programs out there check out the recent molecular modelling newsgroup there was a similar Q posted recently HTH, jez Philippe CHAVATTE wrote: > What is the best methodology to compare two protein 3D structures (pdb > format) ? > What criteria permit to affirm their similarity ? > Many thanks for your help. > > Philippe > > -- > > ----------------- > > Philippe CHAVATTE > Institut de Chimie Pharmaceutique Albert Lespagnol > BP 83 > 59006 LILLE CEDEX > FRANCE > > E-Mail : pchavatt@phare.univ-lille2.fr From owner-proteins@net.bio.net Mon Jul 05 06:39:00 1999 Path: biosci!kfunigraz.ac.at!andreas.kungl From: andreas.kungl@kfunigraz.ac.at (andreas kungl) Newsgroups: bionet.molbio.proteins Subject: 3rd International Conference on Molecular Structural Biology: Last call for Posters Date: 5 Jul 1999 07:39:44 -0700 Organization: Karl-Franzens-Universitaet Graz Lines: 330 Sender: daemon@net.bio.net Distribution: world Message-ID: <3780C0F7.CABAD268@kfunigraz.ac.at> NNTP-Posting-Host: net.bio.net The Biochemistry Subgroup of the Austrian Chemical Society is pleased to announce the Third International Conference on Molecular Structural Biology ICMSB99 which will take place in Vienna, Austria from September 8-12, 1999 FOR DETAILED INFORMATION, PLEASE SEE BELOW OR VISIT OUR HOMEPAGE AT http://www.kfunigraz.ac.at/ipcwww/icmsb99 ************************************************************************ Introduction to the ICMSB99 The First and the Second International Conference on Molecular Structural Biology (ICMSB) took place in Vienna in September 1995 and 1997. Both conferences were very well received by all who took part, including over 250 participants from more than 20 countries worldwide. The organisers are pleased to announce the Third ICMSB, which will take place from 8th to 12th September 1999, and which will, like the previous conferences, feature internationally renowned speakers. The ICMSB99 will focus on topics covering a number of the most exciting areas in the field, with the aim of bringing together specialised scientists from different areas. It will be opened by one of the most outstanding scientists in the field of structural biology, Robert Huber, and the following four days of sessions will include Folding and Function, Novel Structures, Advances in Microscopic Methods, Structural Molecular Biology, Structure-Based Drug Design, and Prediction and Simulation. ************************************************************************ Vienna - An Attractive Conference Location The ICMSB99 will be located at the Federal Chancellery in Vienna. The city is a particularly attractive location for a conference, with its combination of historical buildings, green parks, and modern architecture. Some of the most famous city sights include Schönbrunn Palace and the Hofburg, former homes of the Habsburgs, St. Stephans Cathedral, and the colourful Hundertwasser House. Also unique to Vienna is the Prater park, with its endless green avenues and its funfair, featuring the ´´Riesenrad´´ (ferris wheel). Of course, no trip to Vienna would be complete without a visit to one of the many traditional Viennese cafés, for a piece of the famous Sachertorte. An ´´Oldtimer-Tram´´tour around the Ringstraße will take participants past many of the finest sights. ************************************************************************ Organising Committee A. Kungl, P. Andrew, A. Binder, S. Kristl, A. Schilk ************************************************************************ Scientific Committee C. Kratky, M. Sippl, A. Kungl, P. Andrew ************************************************************************ In Cooperation With Austrian Academy of Sciences Austrian Federal Chancellery Austrian Federal Ministry of Science and Research ************************************************************************ Sponsored By Austrian Airlines Novartis Forschungsinstitut ************************************************************************ Scientific Programme The six sessions of the conference cover a wide range of topics and experimental methods, which will be presented in the form of plenary lectures, selected short oral communications, and posters. Wednesday 8th: Registration from 2 p.m. onwards Evening: Honorary Lecture (followed by a welcome drink and snack) Robert Huber (Max-Planck-Institute, Martinsried): Diversity and Conservation in Proteolytic Enzymes and their Inhibitors Thursday 9th: Morning Session: Advances in Microscopic Methods Werner Kühlbrandt (Max-Planck-Institute, Frankfurt): Two Conformations of Membrane Ion Pumps Hansgeorg Schindler (Linz University): Single Molecule Microscopy Methods for Structural Biology Helen Hansma (University of California, Santa Barbara): Probing Biomaterials with the Atomic Force Microscope Afternoon Session: Folding and Function Alan Fersht (Cambridge University): Minichaperones: Practical and Mechanistic Tools Thomas Kiefhaber (Biozentrum Basel): Speed Limit for Protein Folding Peter Wright (Scripps Institute): Structure and Dynamics of Unfolded Proteins and Protein Folding Intermediates Friday 10th: Morning Session: Novel Structures Michael Rossmann (Purdue University): The Assembly of Viruses Examined by Combining Crystallography and Cryo-electron Microscopy Don Wiley (Harvard University): Structural Studies of Viral Entry Mechanisms in Influenza, HIV-1 and bola Viruses Kurt Wüthrich (ETH Zürich): TROSY and BSE - Recent Progress with NMR in Structural Biology Afternoon Session: Structure-Based Drug Design Siegfried Reich (Agouron Pharmaceuticals): The Use of Protein Structural Information in Drug Design and Development: Some Examples Keith Wilson (Vertex Pharmaceuticals): Structure-Based Drug Design: Reality over Hype Poster Session I Saturday 11th: Morning Session: Structural Molecular Biology Stephen Cusack (EMBL Grenoble): tRNA and Amino Acid Recognition by Aminoacyl-tRNA Synthetases Robert Kaptein (Utrecht University): Allosteric Interactions in Protein-DNA Recognition Christoph Kratky (Graz University): Structure and Mechanism of Enzymes with a B12 Cofactor Paul Sigler (Yale University): Structure and Function in Chaperonin-Assisted Protein Folding Afternoon: Poster Session II (followed by the ´´Oldtimer-Tram´´ tour) Sunday 12th: Morning Session: Structural Genomics David Eisenberg (UCLA): Protein-Protein Interactions Terry Gaasterland (Rockefeller University): Using Patterns of Evolution Across Whole Genomes to Support Structural Genomics Target Selection John Moult (University of Maryland): The Past, Present, and Future of Protein Structure Prediction Wayne Hendrickson (Columbia University): Prospects of High-Throughput Crystallographic Structure Determination Approx. 1 p.m.: End of Conference with Farewell Drink and Snack ************************************************************************ Call for Posters Interested participants are invited to submit abstracts describing original work which has not been presented elsewhere. Abstracts should arrive no later than July 10th, 1999. Authors will be informed about the provisional acceptance of the abstract by the end of July. The presentation of the abstract as a poster will be confirmed, and included in the Book of Abstracts when one or more of the authors registers for the conference. Contributors of outstanding abstracts will be chosen by the Scientific Committee to give a 15 minute oral presentation. Poster Prize A prize of ATS 2,000 will be awarded for the best poster contribution in terms of innovative results and presentation. ************************************************************************ Abstract Submission Camera-ready abstracts should be printed in good quality on a single (A4) sheet of paper, within the area 16 cm wide and 24 cm long. The title should be followed by the author(s) name(s), affiliation(s), and address(es). Text should be in a 12 point font with maximum 1.5 line spacing. Please send two unfolded copies of the abstract to the conference secretariat. ************************************************************************ Posters The poster boards will be 100 cm (width) x 200 cm (height). Materials for poster mounting will be provided. ************************************************************************ Conference Proceedings The lectures and poster presentations will be published by the Austrian Chemical Society in book form (with an ISBN number), and will be distributed to the participants upon arrival at the conference. Additional copies of the Conference Proceedings can be purchased for ATS 300,-. ************************************************************************ General Information Exhibition: An exhibition of instruments, accessories, software, literature, and other items is planned. Companies interested in displaying their products are kindly requested to contact the conference secretariat. Social Events: The conference will be opened by a welcome drink following the honorary lecture in the Federal Chancellery on the evening of Wednesday, September 8th. On Saturday afternoon, the conference participants will be taken on a tram tour of the city centre. Following this, all participants are encouraged to visit a typical Viennese Heurigen (wine cellar) to enjoy the local food and wine (not included in the registration fee). A further social event will be arranged for one other evening, leaving one evening free to explore Vienna. In addition, half day tours to some of Vienna´s best known sights will be organised for accompanying people (dependent on participant number). Registration (please contact the Conference Secretariat or our homepage): Registration Fee Before August 1 After August 1 Regular Participant 5.000 ATS 5.500 ATS GÖCH Member* 4.000 ATS 4.500 ATS Student** 2.500 ATS 3.000 ATS GÖCH-Students*/** 1.750 ATS 2.000 ATS Accompanying Person 500 ATS 600 ATS *Payment must be accompanied by proof of the remittance of the ´99-GÖCH membership fee **Payment must be accompanied by proof of student status The registration desk will be open from 2 p.m. on Wednesday, September 8th. The registration fee includes the Conference Proceedings and participation in all scientific sessions, the welcome and farewell drinks, lunch from Thursday to Saturday, coffee breaks, and participation in the social programme (please note: the Heurigen visit is not included). Accompanying people attend only the social programme (welcome drink, tram tour, additional evening). Accomodation is not included in the registration fee! For accomodation, to register for the Heurigen evening, and to book social events for accompanying people, please ask for the flyer of the travel agency MONDIAL CONGRESS (at the conference secretariat or at our homepage). Remittance of Fees: Remittance must be made in Austrian Schillings (ATS) payable to the Gesellschaft Österreichischer Chemiker, Arbeitsgruppe Biochemie, Account Number 0043-19265/04 at Bank Creditanstalt, Bank Code 11000. Payment is also accepted by sending a (Euro-)Cheque to the conference secretariat or by filling in the credit card form (Visa, Euro/Mastercard, Diners Club, and American Express are accepted). All charges due to bank transfer have to be paid by the sender. The sender´s name and address have to be clearly marked on every remittance. Cancellation: Applications may be cancelled up to August 1st, in which case 85% refund of fees already paid will be made. It will not be possible to offer any refunds if cancellations are made after that date. ************************************************************************ Conference Homepage Please visit our homepage at http://www.kfunigraz.ac.at/ipcwww/icmsb99 for the latest update of the programme plus further information. ************************************************************************ Key Dates July 10, deadline for submitting poster abstracts August 1, deadline for early registration fee August 1, deadline for cancellation ************************************************************************ Location Austrian Federal Chancellery (Bundeskanzleramt) Festsaal Radetzkystraße 2 A-1031 Vienna ************************************************************************ Conference Secretariat Dr. Andreas Kungl Austrian Chemical Society (GÖCH), Biochemistry Subgroupc/o Institute of Pharmaceutical Chemistry University of Graz, Universitätsplatz 1, A-8010 Graz Tel.: +43 316 380 5373, Fax: +43 316 382541 E-Mail: andreas.kungl@kfunigraz.ac.at From owner-proteins@net.bio.net Mon Jul 05 08:46:00 1999 Path: biosci!newshost.lanl.gov!arclight.uoregon.edu!wn4feed!worldnet.att.net!207.172.3.37!feed1.news.rcn.net!rcn!netnews.com!newspeer1.nac.net!newspeer.monmouth.com!nntp2.deja.com!nnrp1.deja.com!not-for-mail From: epsilone@my-deja.com Newsgroups: bionet.molbio.proteins Subject: Immunochemistry : Need picture results for P53, AML-1, c-REL, NFkB and TAL-1 Date: Mon, 05 Jul 1999 16:31:28 GMT Organization: Deja.com - Share what you know. Learn what you don't. Lines: 12 Message-ID: <7lqml0$n51$1@nnrp1.deja.com> NNTP-Posting-Host: 198.164.200.36 X-Article-Creation-Date: Mon Jul 05 12:42:49 1999 GMT X-Http-User-Agent: Mozilla/4.0 (compatible; MSIE 4.01; Windows 98) X-Http-Proxy: 1.0 x40.deja.com:80 (Squid/1.1.22) for client 198.164.200.36 Hi, I would appreciate if someone could send me a picture (or a reference to a web site) of the positive results of an immunochemistry perform on P53, AML-1, c-REL, NFkB and TAL-1. Thank you. Sent via Deja.com http://www.deja.com/ Share what you know. Learn what you don't. From owner-proteins@net.bio.net Mon Jul 05 10:16:00 1999 Path: biosci!gema.org.ar!mcodevilla From: mcodevilla@gema.org.ar ("Maria de los Angeles Codevilla") Newsgroups: bionet.molbio.proteins Subject: Protocol of protein extraction Date: 5 Jul 1999 11:16:10 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 35 Sender: daemon@net.bio.net Distribution: world Message-ID: <000801bec70e$a38933a0$ce00000a@laser> NNTP-Posting-Host: net.bio.net This is a multi-part message in MIME format. ------=_NextPart_000_0005_01BEC6F5.7D27CC80 Content-Type: text/plain; charset="iso-8859-1" Content-Transfer-Encoding: quoted-printable I would like to know where can I find a general protocol for total = protein extraction from bacteria culture. Thanks in advance Maria de los Angeles Codevilla GEMA ------=_NextPart_000_0005_01BEC6F5.7D27CC80 Content-Type: text/html; charset="iso-8859-1" Content-Transfer-Encoding: quoted-printable
I would like to know where can I find a general = protocol for=20 total protein extraction from bacteria culture.
Thanks in advance
Maria de los Angeles Codevilla
GEMA
------=_NextPart_000_0005_01BEC6F5.7D27CC80-- From owner-proteins@net.bio.net Tue Jul 06 03:45:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!logbridge.uoregon.edu!dispose.news.demon.net!demon!news-lond.gip.net!news.gsl.net!gip.net!peer.news.th.u-net.net!u-net!tank.news.pipex.net!pipex!server1.netnews.ja.net!pegasus.csx.cam.ac.uk!hgmp.mrc.ac.uk!biosci From: rvgorsel@mpc186.mpibpc.gwdg.de (Rik van Gorsel) Newsgroups: bionet.molbio.proteins Subject: protein transfer from IEF gels to nitrocellulose for westerns Date: 6 Jul 1999 12:28:39 +0100 Organization: MPI-BPC Message-ID: <3781E856.2DE68D35@mpc186.mpibpc.gwdg.de> NNTP-Posting-Host: mercury.hgmp.mrc.ac.uk Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Trace: niobium.hgmp.mrc.ac.uk 931260519 10777 193.62.192.80 (6 Jul 1999 11:28:39 GMT) X-Complaints-To: news@hgmp.mrc.ac.uk NNTP-Posting-Date: 6 Jul 1999 11:28:39 GMT X-Received: from mserv1.dl.ac.uk (root@mserv1.dl.ac.uk [148.79.160.65]) by hgmp.mrc.ac.uk (8.9.3/8.9.3) with ESMTP id MAA10860 for ; Tue, 6 Jul 1999 12:28:33 +0100 (BST) X-Received: from mpc16189.mpibpc.gwdg.de (mpc16189.mpibpc.gwdg.de [134.76.211.75]) by mserv1.dl.ac.uk with ESMTP id MAA27165 (8.8.8/5.4[ref postmaster@dl.ac.uk] for dl.ac.uk from rvgorsel@mpc186.mpibpc.gwdg.de); Tue, 6 Jul 1999 12:28:32 +0100 (BST) X-Precedence: first-class X-Received: from mpc186.mpibpc.gwdg.de (localhost [127.0.0.1]) by mpc16189.mpibpc.gwdg.de (8.9.1/8.9.1) with ESMTP id NAA03570 for ; Tue, 6 Jul 1999 13:28:23 +0200 (MET DST) X-Reply-To: rvgorsel@mpc186.mpibpc.gwdg.de X-Mailer: Mozilla 4.5 [en] (X11; I; SunOS 5.6 sun4m) X-Accept-Language: en X-To: proteins@dl.ac.uk Lines: 29 Dear electrophoresis specialists, Does anyone know of a good protocol to transfer proteins from IEF gels (Pharmacia PhastSystem) to nitrocellulose for western blotting; one that overcomes the problem of the IEF gel sticking to the nitrocellulose membrane? Is inserting a cellulase acetate membrane between the IEF gel and the nitrocellulose membrane a feasible option? I look forward to any useful suggestions! -- Rik van Gorsel Max Planck Institute for Biophysical Chemistry Department of Molecular Biology Am Fassberg 11 D-37077 Goettingen Germany e-mail: rvgorsel@mpc186.mpibpc.gwdg.de phone: +49-551-201.1388 (office) +49-551-201.1386 (lab) fax: +49-551-201.1467 --- From owner-proteins@net.bio.net Tue Jul 06 05:44:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!news-peer1.sprintlink.net!news-in-central.sprintlink.net!news.sprintlink.net!news1-gui.server.ntli.net!news5-gui.server.ntli.net!ntli.net!server4.netnews.ja.net!server2.netnews.ja.net!pegasus.csx.cam.ac.uk!macg6-5.mrc-lmb.cam.ac.uk!user From: jyl@mrc-lmb.cam.ac.uk (Jan Lowe) Newsgroups: bionet.molbio.proteins Subject: NiNTA-gold conjugates Date: Tue, 06 Jul 1999 14:38:54 +0100 Organization: MRC Laboratory of Molecular Biology Lines: 9 Message-ID: NNTP-Posting-Host: macg6-5.mrc-lmb.cam.ac.uk Hi I would like to label a His6-tagged protein on electron microscopic grids. Anyone any ideas ? A NiNTA molecule conjugated to gold particles would be ideal, but no company is producing those (yet). Thanks, Jan From owner-proteins@net.bio.net Tue Jul 06 05:45:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!news-xfer.newsread.com!netaxs.com!newsread.com!news.temple.edu!tempest.ocis.temple.edu!wjgeese From: Bill Geese Newsgroups: bionet.molbio.proteins Subject: problem dialysing protein Date: Tue, 6 Jul 1999 09:31:35 -0400 Organization: Temple University Lines: 23 Message-ID: NNTP-Posting-Host: tempest.ocis.temple.edu Mime-Version: 1.0 Content-Type: TEXT/PLAIN; charset=US-ASCII X-Sender: wjgeese@tempest.ocis.temple.edu Hi all, I've recently run into some problems with the purification of a his-tagged protein purified over a Ni-NTA agarose column. Specifically, the problem arises during dialysis. After column purification and elution, my protein is in 1M imidazole which I must remove, so I usually dialyze against 0.6L protein storage buffer (40mM Tris(8), 0.1M NaCl, 50% glycerol, 1mM DTT) for 6hr followed by another 6-10hr with a fresh change of dialysis buffer. Normally, following column purification the purified protein solution is clear,however following dialysis, it turns yellow (urine-colored). The longer it's left to dialyze the more intense the yellow color; if left long enough, it eventually turns brown. This is all done at 4C btw. Can anyone offer any insight into my problem? Is this a typical problem during protein purifications? It seems to have only recently been a problem...I havent seen it before. I had been using Snake-skin dialysis membrane by Pierce, which had been replaced with Thomas Scientific membrane, however both have resulted in the same observations. TIA, Bill From owner-proteins@net.bio.net Tue Jul 06 09:15:00 1999 Path: biosci!crbm.cnrs-mop.fr!fesquet From: fesquet@crbm.cnrs-mop.fr (Didier Fesquet) Newsgroups: bionet.molbio.proteins Subject: WESTERN BLOTTING OF 15KDa PRotein Date: 6 Jul 1999 10:15:23 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 26 Sender: daemon@net.bio.net Distribution: world Message-ID: NNTP-Posting-Host: net.bio.net hi, working with a 15KDa protein , we experience difficulties detecting this protein by WB. indeed, we believed that the protein is going throught the nitrocellulose membrane even 0.1micron! . does anybody know how we can sort this out! any help wellcome didier ******************************************************************* Dr Didier FESQUET Centre de Recherche de Biochimie Macromoleculaire CNRS UPR 1086 1919, route de mende 34293 Montpellier cedex 5 (FRANCE) Tel: (33) (0)4-67-61-33-79 ou 33-72 FAX: (33) (0)4-67-52-15-59 From abroad do not dial (0) email: fesquet@crbm.cnrs-mop.fr ************************************************* From owner-proteins@net.bio.net Tue Jul 06 10:05:00 1999 From: Cornelius Krasel Subject: Re: problem dialysing protein Newsgroups: bionet.molbio.proteins References: User-Agent: tin/pre-1.4-19990413 ("Endemoniada") (UNIX) (Linux/2.0.36 (i486)) Date: Tue, 6 Jul 1999 19:24:52 +0200 Message-ID: <45etl7.jh9.ln@wpxx02.toxi.uni-wuerzburg.de> NNTP-Posting-Host: wpxx02.toxi.uni-wuerzburg.de Lines: 22 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!isdnet!newsfeed.tli.de!newsfeed.nacamar.de!uni-erlangen.de!uni-wuerzburg.de!not-for-mail Bill Geese wrote: > After column purification and elution, my protein > is in 1M imidazole which I must remove, so I usually dialyze against 0.6L > protein storage buffer (40mM Tris(8), 0.1M NaCl, 50% glycerol, 1mM DTT) > for 6hr followed by another 6-10hr with a fresh change of dialysis buffer. > Normally, following column purification the purified protein solution is > clear,however following dialysis, it turns yellow (urine-colored). The > longer it's left to dialyze the more intense the yellow color; if left > long enough, it eventually turns brown. This is only a guess but I assume that there is some Ni2+ leaching from your column which is reduced by the DTT in your dialysis buffer. At least a Ni2+ column turns brownish when you run it in a DTT- (or BME-)containing buffer. I would possibly add some EDTA to the protein storage buffer to mop up the Ni2+ which might prevent the problem. --Cornelius. -- /* Cornelius Krasel, U Wuerzburg, Dept. of Pharmacology, Versbacher Str. 9 */ /* D-97078 Wuerzburg, Germany email: phak004@rzbox.uni-wuerzburg.de SP4 */ /* "Science is the game we play with God to find out what His rules are." */ From owner-proteins@net.bio.net Tue Jul 06 12:14:00 1999 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!isdnet!isdnet-serv!not-for-mail From: Maggy Mitra Newsgroups: bionet.molbio.proteins Subject: LAL - endotoxines'level Date: Tue, 06 Jul 1999 22:02:38 +0200 Lines: 6 Message-ID: <378260D9.6446CAE4@worldnet.fr> NNTP-Posting-Host: p13-124.province.worldnet.fr Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Trace: news2.isdnet.net 931291600 10998 195.3.13.124 (6 Jul 1999 20:06:40 GMT) X-Complaints-To: abuse@isdnet.net NNTP-Posting-Date: 6 Jul 1999 20:06:40 GMT X-Mailer: Mozilla 4.01 [en] (Win95; I) X-Priority: 3 (Normal) hi does anyone know the maximum level of endotoxines ( UI/mg of protein) accepted in a human iv injectable vaccin ? Thanks for your help MM From owner-proteins@net.bio.net Tue Jul 06 16:25:00 1999 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!news.maxwell.syr.edu!news.mel.connect.com.au!news.unimelb.edu.au!ludwignt-4 From: murphy_r@licre.ludwig.edu.au (Roger Murphy) Newsgroups: bionet.molbio.proteins Subject: Re: LAL - endotoxines'level Date: Tue, 06 Jul 99 23:21:29 GMT Organization: Ludwig Institute for Cancer Research Lines: 33 Message-ID: <7lu6en$k1v$1@izvestia.its.unimelb.edu.au> References: <378260D9.6446CAE4@worldnet.fr> NNTP-Posting-Host: ludwignt-4.austin.unimelb.edu.au X-Trace: izvestia.its.unimelb.edu.au 931306775 20543 128.250.186.193 (7 Jul 1999 00:19:35 GMT) X-Complaints-To: news@news.unimelb.edu.au NNTP-Posting-Date: 7 Jul 1999 00:19:35 GMT X-Newsreader: News Xpress 2.0 Beta #0 You set the psecififcations on this yourself, but generally you would aim for <100 EU/dose. Note this is PER DOSE, not per mg of protein. The FDA don't care how much protein you're using but they do care about exposure to endotoxin. Of course, it's always much nicer to ensure your chromatographic purification of your protein removes as much endotoxin as possible (anion chromatography, HIC are two good steps for this), and that you are well below your acceptable limit. In article <378260D9.6446CAE4@worldnet.fr>, Maggy Mitra wrote: >hi >does anyone know the maximum level of endotoxines ( UI/mg of protein) >accepted in a human iv injectable vaccin ? >Thanks for your help >MM > ------------------------------------------------------------ Roger Murphy, Ph.D. Biological Production Facility Ludwig Institute for Cancer Research Austin & Repatriation Medical Centre Studley Road, Heidelberg, Vic. 3084 Australia. Tel 61-3-94965463 Fax 61-3-94965436 Email Roger.Murphy@Ludwig.edu.au From owner-proteins@net.bio.net Wed Jul 07 04:21:00 1999 Path: biosci!newshost.lanl.gov!awabi.library.ucla.edu!128.230.129.106!news.maxwell.syr.edu!oleane!jussieu.fr!fu-berlin.de!news.uni-leipzig.de!news.uni-halle.de!not-for-mail From: "Georg Wille" Newsgroups: bionet.molbio.proteins Subject: multimeric lysozyme Date: Wed, 7 Jul 1999 14:03:47 +0200 Organization: University Halle, Germany Lines: 10 Message-ID: <7lvfn6$3fn$1@mlucom4.urz.uni-halle.de> NNTP-Posting-Host: 141.48.48.233 X-Newsreader: Microsoft Outlook Express 4.72.3110.1 X-MimeOLE: Produced By Microsoft MimeOLE V4.72.3110.3 Does anyone know whether it has been described that egg white lysozyme shows a tendency to form multimers (dimers, trimers or even higher order) at elevated protein concentrations? Any information is greatly appreciated! Georg From owner-proteins@net.bio.net Wed Jul 07 08:15:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!news.algonet.se!algonet!newsfeed1.uni2.dk!news.net.uni-c.dk!news.daimi.au.dk!not-for-mail From: Per Mygind Newsgroups: bionet.molbio.proteins Subject: Re: WESTERN BLOTTING OF 15KDa PRotein Date: Wed, 07 Jul 1999 18:03:27 +0200 Organization: University of Aarhus, Department of Computer Science (DAIMI) Lines: 61 Message-ID: <37837A4F.8A9F750C@biobase.dk> References: NNTP-Posting-Host: majestix.gram.au.dk Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Trace: xinwen.daimi.au.dk 931363407 5506330 255.255.255.255 (7 Jul 1999 16:03:27 GMT) X-Complaints-To: news@daimi.au.dk NNTP-Posting-Date: 7 Jul 1999 16:03:27 GMT X-Mailer: Mozilla 4.07 [en] (X11; I; SunOS 5.6 sun4u) Didier Fesquet wrote: > hi, > > working with a 15KDa protein , we experience difficulties detecting this > protein by WB. indeed, we believed that the protein is going throught the > nitrocellulose membrane even 0.1micron! . does anybody know how we can sort > this out! > Try staining the blot with amidoschwartz or similar and also stain the gel upon transfer. Have you tried using nylonmembranes, I don't know if the poresize is different, but the affinity to proteins are superior to the nitrocellulose matrix > > any help wellcome > > didier > > ******************************************************************* > Dr Didier FESQUET > > Centre de Recherche de Biochimie Macromoleculaire > CNRS UPR 1086 > 1919, route de mende > 34293 Montpellier cedex 5 (FRANCE) > Tel: (33) (0)4-67-61-33-79 ou 33-72 > FAX: (33) (0)4-67-52-15-59 > From abroad do not dial (0) > email: fesquet@crbm.cnrs-mop.fr > > ************************************************* -- Kind Regards Per Mygind ************************************************************************ If you are are not part of the solution, you are part of the precipitate ************************************************************************ Per Mygind, Cand.scient Department of Medical Microbiology and Immunology The Bartholin Building, University of Aarhus, Denmark phone : 89 42 17 47, fax : 86 19 61 28 ************************************************************************ It's hard work and great art to make life not so serious ************************************************************************ Life is what happens to you while you're busy making other plans (John Lennon) All you touch and all you see is all your life will ever be (Roger Waters) From owner-proteins@net.bio.net Wed Jul 07 10:27:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!hermes.visi.com!news-out.visi.com!cam-news-hub1.bbnplanet.com!washdc3-snf1!news.gtei.net!news.ums.edu!gamera.cbl.umces.edu!news.umces.edu!cbl.umces.edu!reno From: "Reno T. Nguyen" Newsgroups: bionet.molbio.proteins Subject: Re: multimeric lysozyme Date: Wed, 7 Jul 1999 11:39:23 -0400 Organization: University of Maryland Chesapeake Biological Laboratory Lines: 30 Message-ID: References: <7lvfn6$3fn$1@mlucom4.urz.uni-halle.de> NNTP-Posting-Host: cbl.umces.edu Mime-Version: 1.0 Content-Type: TEXT/PLAIN; charset=US-ASCII X-Trace: gamera.cbl.umces.edu 931361970 8285 131.118.224.6 (7 Jul 1999 15:39:30 GMT) X-Complaints-To: feedback@cbl.umces.edu NNTP-Posting-Date: 7 Jul 1999 15:39:30 GMT To: Georg Wille In-Reply-To: <7lvfn6$3fn$1@mlucom4.urz.uni-halle.de> Hi Georg, When I performed MALDI-TOF MS on lysozyme about two years ago, I did see the presence of dimers. Reno Nguyen On Wed, 7 Jul 1999, Georg Wille wrote: > > Does anyone know whether it has been described that egg white lysozyme shows > a tendency to form multimers (dimers, trimers or even higher order) at > elevated protein concentrations? > ************************************************************************* Reno T. Nguyen Chesapeake Biological Laboratory /----\ /-----\ / Univ. MD Center for Environmental Science / / / / P.O. Box 38 / /______/ / Solomons, MD 20688 / / \ / / / // Tel: (410) 326-7261 \_______/ \_______/ \_______/ (410) 326-7409 Fax: (410) 326-7341 E-mail: reno@cbl.umces.edu ************************************************************************ From owner-proteins@net.bio.net Wed Jul 07 11:46:00 1999 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!news.maxwell.syr.edu!newsfeed.acns.nwu.edu!news.cc.uic.edu!not-for-mail From: Sangkyung Kim Newsgroups: bionet.molbio.proteins Subject: reversible species at Pt electrode Date: Wed, 07 Jul 1999 12:37:31 -0500 Organization: University of Illinois at Chicago Lines: 14 Message-ID: <3783905A.80FE93C8@uic.edu> NNTP-Posting-Host: rumenka.eecs.uic.edu Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 4.51 [en] (WinNT; I) X-Accept-Language: en,ko Hi! I am looking for a good red-ox couple in biological system to test my electrode.I should avoid gaseous products or making layers on the surface of electrode. However any information is welcomed. Could you just toss me some names of biomolecules? Thanks. -- Sangkyung Kim - skim62@uic.edu University of Illinois at Chicago Micro-Actuator Laboratory Department of Bioengineering From owner-proteins@net.bio.net Wed Jul 07 12:57:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!logbridge.uoregon.edu!sunqbc.risq.qc.ca!carnaval.risq.qc.ca.POSTED!not-for-mail From: asheft@po-box.mcgill.ca (Alex Sheftel) Newsgroups: bionet.molbio.proteins Subject: Need help: Western from IEF gel Message-ID: <3784be96.25380793@news.mcgill.ca> X-Newsreader: Forte Agent 1.5/32.452 MIME-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit Lines: 12 Date: Wed, 07 Jul 1999 20:51:25 GMT NNTP-Posting-Host: 206.167.227.2 X-Complaints-To: abuse@mcgill.ca X-Trace: carnaval.risq.qc.ca 931380685 206.167.227.2 (Wed, 07 Jul 1999 16:51:25 EDT) NNTP-Posting-Date: Wed, 07 Jul 1999 16:51:25 EDT Hi, there! I am trying to do western blot after separating protein by thin gel IEF(0.4mm). I would like to know how to transfer protein from IEF gel to nitrocellulose membrane. I found one method that "Netfix has to be used with Gelbond PAG film to strip gel out of the PAG film" It seems to be available from the company named Serva (Heidelburg, Germany). However, I could not locate this company. Does anyone know what Netfix is and where to get this thing? Or does anyone has any other method for western from IEF gel? Thank you very much. From owner-proteins@net.bio.net Wed Jul 07 14:31:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!hermes.visi.com!news-out.visi.com!uunet!chi.uu.net!dfw.uu.net!lax.uu.net!ffx.uu.net!in5.uu.net!news.inter.net.il!not-for-mail From: "Barak Akabayov" Newsgroups: bionet.molbio.proteins Subject: asking for p53 protocols Date: Wed, 7 Jul 1999 22:53:08 +0200 Organization: Internet Gold, ISRAEL Lines: 12 Message-ID: <7m0f03$q7c$1@news2.inter.net.il> NNTP-Posting-Host: r-h-186-141.access.net.il X-Trace: news2.inter.net.il 931381059 26860 192.117.186.141 (7 Jul 1999 20:57:39 GMT) X-Complaints-To: abuse@inter.net.il NNTP-Posting-Date: 7 Jul 1999 20:57:39 GMT X-Priority: 3 X-MSMail-Priority: Normal X-Newsreader: Microsoft Outlook Express 5.00.2014.211 X-MimeOLE: Produced By Microsoft MimeOLE V5.00.2014.211 Dear all: I’m asking for protocol/guide for detection & measurement of p53 in cells (And of course the source which can I achieve the materials). Much appreciate any help ak_barak@internet-zahav.net From owner-proteins@net.bio.net Wed Jul 07 16:14:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!cyclone.bc.net!news.maxwell.syr.edu!newsfeed.cwix.com!152.163.199.19!portc03.blue.aol.com!audrey01.news.aol.com!not-for-mail From: rcjohnsen@aol.com (Rcjohnsen) Newsgroups: bionet.molbio.proteins Subject: Re: asking for p53 protocols Lines: 22 NNTP-Posting-Host: ladder07.news.aol.com X-Admin: news@aol.com Date: 08 Jul 1999 00:08:33 GMT References: <7m0f03$q7c$1@news2.inter.net.il> Organization: AOL http://www.aol.com Mime-Version: 1.0 Content-Type: text/plain; charset=ISO-8859-1 Content-Transfer-Encoding: 8bit Message-ID: <19990707200833.05078.00005134@ng-ck1.aol.com> << Subject: asking for p53 protocols From: "Barak Akabayov" Date: Wed, 07 July 1999 04:53 PM EDT Message-id: <7m0f03$q7c$1@news2.inter.net.il> Dear all: I’m asking for protocol/guide for detection & measurement of p53 in cells (And of course the source which can I achieve the materials). Much appreciate any help ak_barak@internet-zahav.net >> I don't know if this is helpful but go to entrez browzer at http://www3.ncbi.nlm.nih.gov/Entrez/ and click on the literature entry and simple search for p53 detection and measurement. Roger From owner-proteins@net.bio.net Thu Jul 08 07:57:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!news.maxwell.syr.edu!tank.news.pipex.net!pipex!newsfeed.wirehub.nl!surfnet.nl!news.leidenuniv.nl!not-for-mail From: Martijn van Duijn Newsgroups: bionet.molbio.proteins Subject: Electro-elution Date: Thu, 08 Jul 1999 17:45:59 +0200 Organization: University of Leiden The Netherlands Lines: 12 Message-ID: <3784C7B7.210478C7@dds.nl> NNTP-Posting-Host: ruly2s.medfac.leidenuniv.nl Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Trace: highway.leidenuniv.nl 931448698 26527 132.229.11.59 (8 Jul 1999 15:44:58 GMT) X-Complaints-To: usenet@highway.leidenuniv.nl NNTP-Posting-Date: 8 Jul 1999 15:44:58 GMT X-Mailer: Mozilla 4.5 [en] (Win98; I) X-Accept-Language: en Hi, Does anyone know a good protocol for the electro-elution of a protein (30 kD) from excised bands of a polyacrylamide gel? I would like to pool the bands from all slots of a gel, and then concentrate the protein in it for further analysis. The protein I am interested in is an integral membrane protein, in case this causes special problems I should be aware of. Thanks for helping me out! Martijn From owner-proteins@net.bio.net Thu Jul 08 08:53:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!dispose.news.demon.net!demon!baron.netcom.net.uk!netcom.net.uk!server3.netnews.ja.net!news.ox.ac.uk!not-for-mail From: James Cuff Newsgroups: bionet.molbio.proteins Subject: [ANNOUNCE] Secondary structure prediction mail list Date: Thu, 08 Jul 1999 17:47:16 +0100 Organization: European Bioinformatics Institute Message-ID: <3784D614.446B@ebi.ac.uk> NNTP-Posting-Host: worf.molbiol.ox.ac.uk Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Trace: news.ox.ac.uk 931452437 2370 163.1.2.30 (8 Jul 1999 16:47:17 GMT) X-Complaints-To: newsmaster@ox.ac.uk NNTP-Posting-Date: 8 Jul 1999 16:47:17 GMT X-Mailer: Mozilla 3.0 (X11; I; OSF1 V4.0 alpha) Lines: 32 Dear colleagues, We are happy to announce a combined Jpred and secondary structure prediction discussion mailing list. It is planned that the list will act as forum for discussion of protein secondary structure prediction methods and sequence/structure analysis techniques. The mailing list will also be used to keep subscribers up to date with improvements to the Jpred secondary structure prediction WWW server. Announcements of new prediction methods and relevant papers on prediction are also very much welcomed. The jpredusers mailing list can be accessed by sending an e-mail to majordomo@ebi.ac.uk, with the body message containing the words: subscribe jpredusers More information can be found at: http://barton.ebi.ac.uk/ Best regards, James. ----------------------------------------------------------------- James Cuff | European Bioinformatics Institute +44 (0) 1223 49 4607 | Wellcome Trust Genome Campus james@ebi.ac.uk | Hinxton, Cambridge. CB10 1SD, UK ----------------------------------------------------------------- From owner-proteins@net.bio.net Thu Jul 08 10:40:00 1999 Path: biosci!pravda.ucr.edu!not-for-mail From: Alan Williams Newsgroups: bionet.molbio.proteins Subject: Re: WESTERN BLOTTING OF 15KDa PRotein Date: 8 Jul 1999 17:22:41 GMT Organization: University of California, Riverside Lines: 18 Message-ID: <7m2mp1$l2f$1@pravda.ucr.edu> References: <37837A4F.8A9F750C@biobase.dk> NNTP-Posting-Host: batch4165.ucr.edu User-Agent: tin/pre-1.4-981002 ("Phobia") (UNIX) (Linux/2.0.34 (i586)) We have found that drying the blot overnight at room temp after transfer greatly improves detection (and presumably retention of the proteins on the membrane) for a set of small acidic proteins that we work with. We are using 0.2 micron membranes. : Didier Fesquet wrote: :> working with a 15KDa protein , we experience difficulties detecting this :> protein by WB. indeed, we believed that the protein is going throught the :> nitrocellulose membrane even 0.1micron! . does anybody know how we can sort :> this out! ************************************************************************ Alan Williams ------------------------------------------------------------------------ University of California, Riverside "Where observation is concerned, Dept. of Botany and Plant Sciences chance favors the prepared mind." Alan@TheWilliamsFamily.org -- Louis Pasteur ************************************************************************ From owner-proteins@net.bio.net Thu Jul 08 10:51:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!nntp.primenet.com!nntp.gctr.net!in1.nntp.cais.net!199.0.216.204.MISMATCH!audrey2.cais.com!not-for-mail From: ZZZkencates@webzone.net (Ken Cates) Newsgroups: sci.med.nutrition,bionet.molbio.proteins,alt.support.diet.low-carb,alt.support.diet.low-fat Subject: Excess proteins in diet Message-ID: <3785eda4.4025022@news3.webzone.net> X-Newsreader: Forte Agent 1.5/32.451 X-No-Archive: yes MIME-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit Lines: 25 Date: Thu, 08 Jul 1999 18:45:03 GMT NNTP-Posting-Host: 208.137.187.92 X-Trace: audrey2.cais.com 931460159 208.137.187.92 (Thu, 08 Jul 1999 14:55:59 EDT) NNTP-Posting-Date: Thu, 08 Jul 1999 14:55:59 EDT Organization: CAIS Internet I believe that protein in the human diet is normally used to repair and maintain bodily structures: build and repair muscles, aid in healing, etc. I further believe that, in times of carbohydrate deprivation, proteins can be deaminated and thus transformed into carbohydrates that are then available for use in the central nervous system. Given this, I have two questions: 1) What, if any, are the further uses of protein in the human body? 2) During times of dietary plenty, when there is an over-abundance of carbohydrates, proteins, and fats in the human diet, what happens to the excess carbohydrates? How are they utilized or disposed of? What is the mechanism? Thanks in advance for any help, -- Ken Return e-mail address is bogus to foil spammer robots. Please remove ZZZ from return address to reply. From owner-proteins@net.bio.net Thu Jul 08 12:13:00 1999 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!newsfeed.direct.ca!tor-nx1.netcom.ca!beaker.tor.sfl.net!bunson.tor.sfl.net!not-for-mail From: "Achim Recktenwald, PhD" Newsgroups: bionet.molbio.proteins References: <378260D9.6446CAE4@worldnet.fr> <7lu6en$k1v$1@izvestia.its.unimelb.edu.au> Subject: Re: LAL - endotoxines'level Lines: 33 X-Priority: 3 X-MSMail-Priority: Normal X-Newsreader: Microsoft Outlook Express 5.00.2314.1300 X-MimeOLE: Produced By Microsoft MimeOLE V5.00.2314.1300 Message-ID: Date: Thu, 08 Jul 1999 20:07:20 GMT NNTP-Posting-Host: 139.142.212.35 NNTP-Posting-Date: Thu, 08 Jul 1999 16:07:20 EST Roger Murphy wrote in message news:7lu6en$k1v$1@izvestia.its.unimelb.edu.au... > You set the psecififcations on this yourself, but generally you would aim for > <100 EU/dose. > > Note this is PER DOSE, not per mg of protein. The FDA don't care how much > protein you're using but they do care about exposure to endotoxin. > > Of course, it's always much nicer to ensure your chromatographic purification > of your protein removes as much endotoxin as possible (anion chromatography, > HIC are two good steps for this), and that you are well below your acceptable > limit. > In a different newsgroup I just answered to the same post. Just to add something to Roger's answer: Another good method to get rid of endotoxin is IMAC, e.g., Chelating Sepharose. Quite a lot of proteins are able to bind to this kind of resin, not only those with a poly-his tag. Other residues than histidine can bind to IMAC-resins, as well. We use this method routinely to wash off endotoxin. Cheers, Achim From owner-proteins@net.bio.net Thu Jul 08 12:56:00 1999 Path: biosci!newshost.lanl.gov!awabi.library.ucla.edu!128.230.129.106!news.maxwell.syr.edu!newsfeed.mathworks.com!newsfeed1.earthlink.net!nntp.earthlink.net!posted-from-earthlink!not-for-mail From: "Toni" Newsgroups: sci.med.nutrition,bionet.molbio.proteins,alt.support.diet.low-carb,alt.support.diet.low-fat Subject: Re: Excess proteins in diet Date: Thu, 8 Jul 1999 16:36:18 -0400 References: <3785eda4.4025022@news3.webzone.net> X-Posted-Path-Was: not-for-mail X-Priority: 3 X-Mimeole: Produced By Microsoft MimeOLE V5.00.2014.211 X-ELN-Date: 8 Jul 1999 20:35:48 GMT X-ELN-Insert-Date: Thu Jul 8 13:45:02 1999 Organization: EarthLink Network, Inc. X-Newsreader: Microsoft Outlook Express 5.00.2014.211 X-MSMail-Priority: Normal Lines: 17 Reply-To: "Toni" NNTP-Posting-Host: sdn-ar-004flflaup187.dialsprint.net Message-ID: <7m3234$rl4$1@oak.prod.itd.earthlink.net> > 2) During times of dietary plenty, when there is an > over-abundance of carbohydrates, proteins, and fats in the human > diet, what happens to the excess carbohydrates? How are they > utilized or disposed of? What is the mechanism? > Can't speak for anyone else, but all the extra carbohydrates I ever ate are living happily on my ass! -- Toni 216/194/142 www.irish-wolfhounds.com ToniATirish-wolfhoundsDOTcom From owner-proteins@net.bio.net Thu Jul 08 18:20:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!cyclone.swbell.net!uunet!ffx.uu.net!news.optonline.net!not-for-mail From: "JK Sinrod" Newsgroups: sci.med.nutrition,bionet.molbio.proteins,alt.support.diet.low-carb,alt.support.diet.low-fat References: <3785eda4.4025022@news3.webzone.net> <7m3234$rl4$1@oak.prod.itd.earthlink.net> Subject: Re: Excess proteins in diet Lines: 32 X-Priority: 3 X-MSMail-Priority: Normal X-Newsreader: Microsoft Outlook Express 5.00.2314.1300 X-MimeOLE: Produced By Microsoft MimeOLE V5.00.2314.1300 Message-ID: Date: Fri, 09 Jul 1999 02:14:30 GMT NNTP-Posting-Host: 167.206.230.89 NNTP-Posting-Date: Thu, 08 Jul 1999 22:14:30 EDT Organization: Optimum Online Maybe an ass-eviction would help? LOL -- 256/245/218/185 15 weeks Atkins Sinrod Stained Glass Studios http://members.aol.com/JKSinrod/sinrod.html Coney Island Memories http://members.aol.com/JKSinrod/page4.html Toni wrote in message news:7m3234$rl4$1@oak.prod.itd.earthlink.net... > > > 2) During times of dietary plenty, when there is an > > over-abundance of carbohydrates, proteins, and fats in the human > > diet, what happens to the excess carbohydrates? How are they > > utilized or disposed of? What is the mechanism? > > > Can't speak for anyone else, but all the extra carbohydrates I ever ate are > living happily on my ass! > > -- > Toni > 216/194/142 > www.irish-wolfhounds.com > ToniATirish-wolfhoundsDOTcom > > > > From owner-proteins@net.bio.net Thu Jul 08 18:24:00 1999 Message-ID: <37855BAE.48C97F0A@IntoThe.Net> Date: Thu, 08 Jul 1999 19:17:22 -0700 From: Mark Reply-To: Mark@IntoThe.Net X-Mailer: Mozilla 4.61 (Macintosh; I; PPC) X-Accept-Language: en-US MIME-Version: 1.0 Newsgroups: sci.med.nutrition,bionet.molbio.proteins,alt.support.diet.low-carb Subject: Re: Excess proteins in diet References: <3785eda4.4025022@news3.webzone.net> <7m3234$rl4$1@oak.prod.itd.earthlink.net> Content-Type: text/plain; charset=us-ascii; x-mac-type="54455854"; x-mac-creator="4D4F5353" Content-Transfer-Encoding: 7bit NNTP-Posting-Host: 208.25.57.124 X-Original-NNTP-Posting-Host: 208.25.57.124 X-Trace: 9 Jul 1999 03:02:09 -0700, 208.25.57.124 Lines: 18 X-Original-NNTP-Posting-Host: 209.63.224.240 Path: biosci!newshost.lanl.gov!awabi.library.ucla.edu!128.32.206.55!newsfeed.berkeley.edu!remarQ73!supernews.com!remarQ.com!nuq-peer.news.verio.net!newsfeed.easynews.com!easynews!news-west.eli.net!news1.jps.net!208.25.57.124 Yes, that is a good one. mine are on my ass, too! Toni wrote: > > 2) During times of dietary plenty, when there is an > > over-abundance of carbohydrates, proteins, and fats in the human > > diet, what happens to the excess carbohydrates? How are they > > utilized or disposed of? What is the mechanism? > > > Can't speak for anyone else, but all the extra carbohydrates I ever ate are > living happily on my ass! > > -- > Toni > 216/194/142 > www.irish-wolfhounds.com > ToniATirish-wolfhoundsDOTcom From owner-proteins@net.bio.net Thu Jul 08 18:54:00 1999 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!news.maxwell.syr.edu!newsfeed.atl!upstream.atl!news2.atl.POSTED!not-for-mail Message-ID: <37852A68.38D20773@bellsouth.net> From: Debra Long X-Mailer: Mozilla 4.04 [en]C-bls40 (Win95; U) MIME-Version: 1.0 Newsgroups: sci.med.nutrition,bionet.molbio.proteins,alt.support.diet.low-carb Subject: Re: Excess proteins in diet References: <3785eda4.4025022@news3.webzone.net> <7m3234$rl4$1@oak.prod.itd.earthlink.net> <37855BAE.48C97F0A@IntoThe.Net> Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit Lines: 27 Date: Thu, 08 Jul 1999 22:47:05 +0000 NNTP-Posting-Host: 209.214.171.164 X-Trace: news2.atl 931488476 209.214.171.164 (Thu, 08 Jul 1999 22:47:56 EDT) NNTP-Posting-Date: Thu, 08 Jul 1999 22:47:56 EDT ...hips, ass, breast, thighs, yada, yada, yada. Too bad none of them landed on my brain. ;) Mark wrote: > > Yes, that is a good one. mine are on my ass, too! > > Toni wrote: > > > > 2) During times of dietary plenty, when there is an > > > over-abundance of carbohydrates, proteins, and fats in the human > > > diet, what happens to the excess carbohydrates? How are they > > > utilized or disposed of? What is the mechanism? > > > > > Can't speak for anyone else, but all the extra carbohydrates I ever ate are > > living happily on my ass! > > > > -- > > Toni > > 216/194/142 > > www.irish-wolfhounds.com > > ToniATirish-wolfhoundsDOTcom -- 180/151.5(Total Loss 28.5+10 muscle gain=38.5 to date)/125/ 550 Levis: 14/8/5 BF%:?/28.1%/15%? B: 44F/36DD/32C W:36/27.5/20 H:40/33/30 Thighs:28/23/20 FAQ PAGE: http://www.grossweb.com/asdlc/ From owner-proteins@net.bio.net Thu Jul 08 20:06:00 1999 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!sunqbc.risq.qc.ca!news.uow.edu.au!news.usyd.edu.au!unsw.edu.au!not-for-mail From: Scott Craig Newsgroups: bionet.molbio.proteins Subject: Re: NiNTA-gold conjugates Date: Fri, 09 Jul 1999 13:45:21 +1000 Organization: School of Biotechnology, University of New South Wales Lines: 22 Message-ID: <37857051.72289543@student.unsw.edu.au> References: NNTP-Posting-Host: 149.171.144.202 Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 4.6 [en] (Win95; I) X-Accept-Language: en Hi Jan, What about a mouse anti-His primary antibody with anti-mouse:gold secondary Jan Lowe wrote: > Hi > > I would like to label a His6-tagged protein on electron microscopic > grids. Anyone any ideas ? A NiNTA molecule conjugated to gold particles > would be ideal, but no company is producing those (yet). > > Thanks, > > Jan -- Scott Craig Dept. of Biotechnology University of New South Wales Sydney, Australia From owner-proteins@net.bio.net Thu Jul 08 20:26:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!nntp.primenet.com!nntp.gctr.net!in1.nntp.cais.net!199.0.216.204.MISMATCH!audrey2.cais.com!not-for-mail From: ZZZkencates@webzone.net (Ken Cates) Newsgroups: sci.med.nutrition,bionet.molbio.proteins,alt.support.diet.low-carb,alt.support.diet.low-fat Subject: Excess *proteins* in diet (Repost - excuse the typo) Message-ID: <378577c3.14050100@news3.webzone.net> X-Newsreader: Forte Agent 1.5/32.451 X-No-Archive: yes MIME-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit Lines: 25 Date: Fri, 09 Jul 1999 04:19:56 GMT NNTP-Posting-Host: 208.152.103.53 X-Trace: audrey2.cais.com 931494652 208.152.103.53 (Fri, 09 Jul 1999 00:30:52 EDT) NNTP-Posting-Date: Fri, 09 Jul 1999 00:30:52 EDT Organization: CAIS Internet I believe that protein in the human diet is normally used to repair and maintain bodily structures: build and repair muscles, aid in healing, etc. I further believe that, in times of carbohydrate deprivation, proteins can be deaminated and thus transformed into carbohydrates that are then available for use in the central nervous system. Given this, I have two questions: 1) What, if any, are the further uses of protein in the human body? 2) During times of dietary plenty, when there is an over-abundance of carbohydrates, proteins, and fats in the human diet, what happens to the excess *proteins*? How are they utilized or disposed of? What is the mechanism? Thanks in advance for any help, -- Ken Return e-mail address is bogus to foil spammer robots. Please remove ZZZ from return address to reply. From owner-proteins@net.bio.net Thu Jul 08 23:15:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!dispose.news.demon.net!demon!newsfeed.nacamar.de!newsfeed.nacamar.de!newscore.univie.ac.at!newsfeed03.univie.ac.at!news.univie.ac.at!not-for-mail From: a8803349.nospam@unet.univie.ac.at (Martin Offterdinger) Newsgroups: bionet.molbio.proteins Subject: Re: WESTERN BLOTTING OF 15KDa PRotein Date: Fri, 09 Jul 1999 06:38:08 GMT Organization: AKH Message-ID: <3785983f.2956228@news.univie.ac.at> References: <37837A4F.8A9F750C@biobase.dk> <7m2mp1$l2f$1@pravda.ucr.edu> NNTP-Posting-Host: grunt.imed1.akh-wien.ac.at X-Trace: www.univie.ac.at 931504146 19254 149.148.97.3 (9 Jul 1999 07:09:06 GMT) X-Complaints-To: news-adm@news.univie.ac.at NNTP-Posting-Date: 9 Jul 1999 07:09:06 GMT X-Newsreader: Forte Free Agent 1.1/16.230 Lines: 32 On 8 Jul 1999 17:22:41 GMT, Alan Williams wrote: >We have found that drying the blot overnight at room temp after transfer >greatly improves detection (and presumably retention of the proteins on the >membrane) for a set of small acidic proteins that we work with. We are >using 0.2 micron membranes. > >: Didier Fesquet wrote: >:> working with a 15KDa protein , we experience difficulties detecting this >:> protein by WB. indeed, we believed that the protein is going throught the >:> nitrocellulose membrane even 0.1micron! . does anybody know how we can sort >:> this out! > >************************************************************************ >Alan Williams >------------------------------------------------------------------------ >University of California, Riverside "Where observation is concerned, >Dept. of Botany and Plant Sciences chance favors the prepared mind." >Alan@TheWilliamsFamily.org -- Louis Pasteur >************************************************************************ Maybe you should also try using PVDF membranes, they generally have a higher affinity than nitroc.; let the membrane dry after transfer; another option is using PVDF-protein sequencing membranes (Millipore) they have a very high protein binding capacity. Martin Offterdinger Martin Offterdinger Internal Med.I,Dept. Oncology University of Vienna Austria E-Mail:a8803349.nospam@unet.univie.ac.at (remove .nospam before mailing) From owner-proteins@net.bio.net Fri Jul 09 05:26:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!news.maxwell.syr.edu!ameritech.net!nntp0.chicago.il.ameritech.net.POSTED!not-for-mail From: "rosie@readandpost" Newsgroups: sci.med.nutrition,bionet.molbio.proteins,alt.support.diet.low-carb,alt.support.diet.low-fat References: <3785eda4.4025022@news3.webzone.net> <7m3234$rl4$1@oak.prod.itd.earthlink.net> Subject: Re: Excess proteins in diet Lines: 18 Organization: rosie@readandpost MIME-Version: 1.0 Content-Type: text/plain; charset="iso-8859-1" Content-Transfer-Encoding: 7bit X-Newsreader: Microsoft Outlook Express 4.72.3155.0 X-MimeOLE: Produced By Microsoft MimeOLE V4.72.3155.0 Message-ID: Date: Fri, 9 Jul 1999 08:17:49 -0500 NNTP-Posting-Host: 209.18.22.53 X-Trace: nntp0.chicago.il.ameritech.net 931527027 209.18.22.53 (Fri, 09 Jul 1999 08:30:27 CDT) NNTP-Posting-Date: Fri, 09 Jul 1999 08:30:27 CDT >Can't speak for anyone else, but all the extra carbohydrates I ever ate are >living happily on my ass! > >-- >Toni >216/194/142 >www.irish-wolfhounds.com >ToniATirish-wolfhoundsDOTcom > > ROTFLMAO! ( i wish is was LMAO!!!!!!) > > From owner-proteins@net.bio.net Fri Jul 09 11:31:00 1999 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!nuq-peer.news.verio.net!nntp.primenet.com!nntp.gctr.net!in1.nntp.cais.net!199.0.216.204.MISMATCH!audrey2.cais.com!not-for-mail From: ZZZkencates@webzone.net (Ken Cates) Newsgroups: bionet.molbio.proteins Subject: Excess *proteins* in diet (Repost - please excuse the typo) Message-ID: <37894c6f.17436581@news3.webzone.net> X-Newsreader: Forte Agent 1.5/32.451 X-No-Archive: yes MIME-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit Lines: 25 Date: Fri, 09 Jul 1999 19:25:08 GMT NNTP-Posting-Host: 208.152.100.195 X-Trace: audrey2.cais.com 931548960 208.152.100.195 (Fri, 09 Jul 1999 15:36:00 EDT) NNTP-Posting-Date: Fri, 09 Jul 1999 15:36:00 EDT Organization: CAIS Internet I believe that protein in the human diet is normally used to repair and maintain bodily structures: build and repair muscles, aid in healing, etc. I further believe that, in times of carbohydrate deprivation, proteins can be deaminated and thus transformed into carbohydrates that are then available for use in the central nervous system. Given this, I have two questions: 1) What, if any, are the further uses of protein in the human body? 2) During times of dietary plenty, when there is an over-abundance of carbohydrates, proteins, and fats in the human diet, what happens to the excess *proteins*? How are they utilized or disposed of? What is the mechanism? Thanks in advance for any help, -- Ken Return e-mail address is bogus to foil spammer robots. Please remove ZZZ from return address to reply. From owner-proteins@net.bio.net Sat Jul 10 00:20:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!dispose.news.demon.net!demon!easynet-tele!easynet.net!tank.news.pipex.net!pipex!server1.netnews.ja.net!hgmp.mrc.ac.uk!mlush From: mlush@hgmp.mrc.ac.uk (Mr. M.J. Lush) Newsgroups: bionet.molbio.proteins Subject: Re: Excess *proteins* in diet (Repost - please excuse the typo) Date: 10 Jul 1999 08:14:26 GMT Organization: UK HGMP Resource Centre Message-ID: <7m6vd2$i05$1@niobium.hgmp.mrc.ac.uk> References: <37894c6f.17436581@news3.webzone.net> NNTP-Posting-Host: tin.hgmp.mrc.ac.uk X-Trace: niobium.hgmp.mrc.ac.uk 931594466 18437 193.62.192.50 (10 Jul 1999 08:14:26 GMT) X-Complaints-To: news@hgmp.mrc.ac.uk NNTP-Posting-Date: 10 Jul 1999 08:14:26 GMT Lines: 13 In article <37894c6f.17436581@news3.webzone.net>, Ken Cates wrote: >I believe that protein in the human diet is normally used to > >Given this, I have two questions: Or perhaps more accuractly your teacher has two questions? -- Michael ~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ NPC rights activist | Nameless Abominations are people too. From owner-proteins@net.bio.net Sat Jul 10 06:12:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!paloalto-snf1.gtei.net!pulsar.dimensional.com!dimensional.com!hermes.visi.com!news-out.visi.com!cam-news-hub1.bbnplanet.com!washdc3-snh1.gtei.net!news.gtei.net!dfiatx1-snr1.gtei.net.POSTED!not-for-mail From: rbales@gte.net (Ron Bales) Newsgroups: sci.med.nutrition,bionet.molbio.proteins,alt.support.diet.low-carb,alt.support.diet.low-fat Subject: Re: Excess proteins in diet Reply-To: rbales@gte.net Message-ID: <378a523a.5742531@news.gte.net> References: <3785eda4.4025022@news3.webzone.net> <7m3234$rl4$1@oak.prod.itd.earthlink.net> X-Newsreader: Forte Agent 1.5/32.452 MIME-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit Lines: 15 X-Trace: /w/U24RAsV9cGLbVSIM3mQaya2tJNkcxbzi6j+S62jQONHv92LelIN8kjOLeb6/yQxSrnTql6BGB!oAoEORZyB7HI7GTOFrYT3OPYda/1C9K0RcUgv7WzS7d5jIVCCvTSCv4= X-Complaints-To: abuse@gte.net X-Abuse-Info: Please be sure to forward a copy of ALL headers X-Abuse-Info: Otherwise we will be unable to process your complaint properly NNTP-Posting-Date: Sat, 10 Jul 1999 14:06:26 GMT Distribution: world Date: Sat, 10 Jul 1999 14:06:26 GMT On Thu, 8 Jul 1999 16:36:18 -0400, "Toni" wrote: > >> 2) During times of dietary plenty, when there is an >> over-abundance of carbohydrates, proteins, and fats in the human >> diet, what happens to the excess carbohydrates? How are they >> utilized or disposed of? What is the mechanism? >> >Can't speak for anyone else, but all the extra carbohydrates I ever ate are >living happily on my ass! Precise, to the point and using only plain language. ROn From owner-proteins@net.bio.net Sun Jul 11 17:15:00 1999 Path: biosci!ust.hk!bchmc From: bchmc@ust.hk ("H.M. CHEN") Newsgroups: bionet.molbio.proteins Subject: Postdoctoral Fellow Date: 11 Jul 1999 18:15:24 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 20 Sender: daemon@net.bio.net Distribution: world Message-ID: NNTP-Posting-Host: net.bio.net ----------------------------------------------------------------------- We have immediate opening for a Postdoctoral Fellow. Membrane lysis of custom anti-bacterial peptides on lipid bilayers (liposomes) (reference see Wang et al., JBC, 273:27438-27448, 1998). Ph.D. required. Salary: US$35,000 per annum. One year term but may be renewable. Send Curriculum Vitae and name of three references to (e-mail preferred): Dr. HM Chen, Department of Biochemistry, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong. Tel:(852)2358-7294; Fax:(852)2358-1552; e-mail:bchmc@ust.hk Everyone whose research qualifications match our project requirement will be considered. The medium in Hong Kong is English. Please have your response as soon as possible. Thanks a lot for your attention. ---------------------------------------------------------------------------- From owner-proteins@net.bio.net Sun Jul 11 19:09:00 1999 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!newsfeed.direct.ca!novia!newsfeed.gol.com!wnoc-tyo-news!news.join.ad.jp!news-sv.sinet!news.nc.u-tokyo.ac.jp!gray.ims.u-tokyo.ac.jp!not-for-mail From: RECOMB 2000 Newsgroups: bionet.molbio.proteins Subject: RECOMB 2000 Date: Mon, 12 Jul 1999 12:00:06 +0900 Organization: Human Genome Center, Inst. of Medical Science, Univ. of Tokyo, Japan. Lines: 211 Message-ID: <37895A36.BC83CAD4@ims.u-tokyo.ac.jp> NNTP-Posting-Host: pine.ims.u-tokyo.ac.jp Mime-Version: 1.0 Content-Type: text/plain; charset=iso-2022-jp Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 4.6 [ja] (Win95; I) X-Accept-Language: ja FIRST CALL FOR PAPERS FOURTH ANNUAL INTERNATIONAL CONFERENCE ON COMPUTATIONAL MOLECULAR BIOLOGY (RECOMB 2000) April 8-11, 2000 Tokyo, Japan Organized by Human Genome Center, Institute of Medical Science, University of Tokyo Sponsored by ACM (Association for Computing Machinery) - SIGACT with support from Compugen IBM Corporation International Society for Computational Biology SLOAN Foundation SmithKline Beecham US National Science Foundation US Department of Energy http://recomb2000.ims.u-tokyo.ac.jp The Fourth Annual Conference on Research in Computational Molecular Biology (RECOMB 2000), sponsored by the Association for Computing Machinery Special Interest Group on Algorithms and Computation Theory (ACM-SIGACT) with support from the SLOAN Foundation, US Department of Energy, US National Science Foundation, SmithKline Beecham, IBM Corporation, Compugen and ISCB will be organized by HGC, Institute of Medical Science, University of Tokyo, in Tokyo, Japan on April 8-11, 2000. The conference will be held at the Tokyo Big Sight International Exhibition Center. Papers reporting on original research (both theoretical and experimental) in all areas of computational molecular biology are sought, including surveys of important recent results/directions. Typical but not exclusive topics of interest include: - Genomics, - Molecular sequence analysis, - Recognition of genes and regulatory elements, - Molecular evolution, - Protein structure, - Gene Expression, - Gene Networks, - Combinatorial libraries and drug design, - Computational proteomics, - Functional genomics. ABSTRACT SUBMISSION: Authors are encouraged to submit their abstracts ELECTRONICALLY. Electronic submission instructions can be found at http://sigact.csci.unt.edu/~recomb2k/RECOMB2000.html. Authors who are unable to do so are requested to send 10 copies (preferably two sided copies) to: Prof. Ron Shamir RECOMB 2000 Program Chair Department of Computer Science Tel Aviv University Tel Aviv, 69978 Israel shamir@math.tau.ac.il An abstract must be received by September 30 1999, 23:59 EST. This is a firm deadline. Simultaneous submission to another conference or journal is allowed. Authors should inform the program chair at the time of submission of the simultaneous submission. CONFERENCE PROCEEDINGS: The extended abstracts for the Conference will be published by ACM Press and will be available at the Conference. A selection of the accepted extended abstracts in their final journal versions will be invited to appear in a special issue of the Journal of Computational Biology devoted to RECOMB 2000. NOTIFICATION: The conference submissions will be refereed by the program committee. Authors will be notified of acceptance or rejection by a letter mailed on or before December 5, 1999. A final copy of each accepted paper is required by January 5, 2000. An author of each accepted paper is expected to attend the Symposium and present the paper; otherwise alternative arrangements should be made to have the paper presented. ABSTRACT PREPARATION: An abstract should start with a succinct statement of the problem, the results achieved, their significance and a comparison with previous work. This material should be understandable to non-specialists. A technical exposition directed to the specialist should follow. The length, excluding cover page and bibliography, should not exceed 10 pages. The manuscript should be easy to read, using at least 11 point font size on U.S. standard 8 1/2 by 11 inch paper with no less than one inch margin all around. If authors believe that more details are absolutely necessary to substantiate the claims of the paper, they may include a clearly marked appendix. An E-mail address for the contact author should be included. Abstracts that deviate significantly from these guidelines risk rejection without consideration of their merits. POSTERS: RECOMB 2000 will include a poster session. Accepted posters will appear in a special poster book published by the Human Genome Center, University of Tokyo. Poster submission instructions will be announced later. CONFERENCE EVENTS: RECOMB 2000 will feature 9 Plenary Lectures (to be announced later) including the following conference events: - The Stanislaw Ulam Memorial Computational Biology Address: awarded by RECOMB to a scientist who has made major contributions in the computational aspects of the field. - The Distinguished Biology Lecture: awarded by RECOMB to a scientist who has made major contributions in the biological aspects of the field. - The Distinguished New Technologies Lecture: describing emerging, new technologies. - Best Paper by a Young Scientist Award: This award will be given to the best paper written solely by one or more recent graduates or students. An abstract is eligible if all authors are recent graduates (within 3 years from Ph.D.) or full-time students at the time of submission. This should be indicated in a letter to the program chair that accompanies the submission. The program committee may decline to make the award or may split it among several papers. CALENDAR Deadline for submission of papers: September 30th, 1999 Notification of acceptance/rejection: December 5th, 1999 Deadline for reception of final papers: January 5th, 2000 STEERING COMMITTEE Sorin Istrail, RECOMB General Vice-Chair Sandia National Laboratories, USA Richard Karp University of California, Berkeley, USA Thomas Lengauer GMD-SCAI, Germany Pavel Pevzner, RECOMB General Chair University of Southern California, USA Ron Shamir Tel-Aviv University, Israel Michael Waterman, RECOMB General Chair University of Southern California, USA PROGRAM COMMITTEE Steve Bryant NCBI, USA Andrea Califano IBM, USA Gordon Crippen University of Michigan, Ann Arbor, USA Ken Dill University of California San Francisco Richard Durbin Sanger Centre, UK Jim Fickett SmithKline Beecham, USA Phil Green University of Washington, Seattle, USA Dan Gusfield University of California, Davis, USA Sorin Istrail Sandia National Laboratories, USA Richard Karp University of California, Berkeley, USA Jonathan King MIT, USA George Komatsoulis Human Genome Sciences, USA Thomas Lengauer GMD-SCAI, Germany Michael Levitt Stanford University, USA Satoru Miyano University of Tokyo, Japan Pavel Pevzner University of Southern California, USA Gesine Reinert King's College, Cambridge, UK David Sankoff University of Montreal, Canada Ron Shamir, Program Committee Chair Tel-Aviv University, Israel Donna Slonim Whitehead Institute, USA Temple Smith Boston University, USA Mike Steel University of Canterbury, New Zealand Martin Vingron DKFZ, Heidelberg, Germany Lusheng Wang City University of Hong Kong, China Michael Waterman University of Southern California, USA Erik Winfree Princeton University, USA Haim Wolfson Tel Aviv University, Israel ORGANIZING COMMITTEE: Tatsuya Akutsu, Publicity Chair HGC, University of Tokyo, Japan Nir Friedman Hebrew University, Israel Osamu Maruyama HGC, University of Tokyo, Japan Satoru Miyano, Organizing Committee Chair HGC, University of Tokyo, Japan Kenta Nakai HGC, University of Tokyo, Japan Asako Suzuki, Registration Chair HGC, University of Tokyo, Japan Ayako Tomiyasu HGC, University of Tokyo, Japan Toshihisa Takagi, Treasurer HGC, University of Tokyo, Japan INFORMATION Human Genome Center Institute of Medical Science University of Tokyo 4-6-1 Shirokanedai, Minato-ku Tokyo 108-8639, Japan Phone: +81-3-5449-5615 Fax: +81-3-5449-5442 email : recomb2000@ims.u-tokyo.ac.jp http://recomb2000.ims.u-tokyo.ac.jp From owner-proteins@net.bio.net Mon Jul 12 01:36:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!uchinews2!yellow.newsread.com!netaxs.com!newsread.com!newspeer1.nac.net!news.maxwell.syr.edu!nntp2.deja.com!nnrp1.deja.com!not-for-mail From: Kresten Newsgroups: bionet.molbio.proteins Subject: Re: multimeric lysozyme Date: Mon, 12 Jul 1999 09:17:21 GMT Organization: Deja.com - Share what you know. Learn what you don't. Lines: 33 Message-ID: <7mcbqs$ikj$1@nnrp1.deja.com> References: <7lvfn6$3fn$1@mlucom4.urz.uni-halle.de> NNTP-Posting-Host: 130.226.1.36 X-Article-Creation-Date: Mon Jul 12 09:17:21 1999 GMT X-Http-User-Agent: Mozilla/4.5 [en] (Win95; I) X-Http-Proxy: 1.0 www2.crc.dk:3128 (Squid/2.1.RELEASE),NetCache@www-cache: Version 3.3.1, 1.0 x36.deja.com:80 (Squid/1.1.22) for client 130.226.182.217, 130.226.1.36 I once ran an SDS-gel of an NMR-sample of HEWL and saw several multimeric species. Don't know whether my reduction/denaturation wasn't good enough or whether the multimers are really stable. The concentration in the NMR sample was of course rather high and so was pH. Also I think has has been some papers of amyloidogenic variants of lysozyme from Dobsons group IIRC. hth Kresten In article <7lvfn6$3fn$1@mlucom4.urz.uni-halle.de>, "Georg Wille" wrote: > Does anyone know whether it has been described that egg white lysozyme shows > a tendency to form multimers (dimers, trimers or even higher order) at > elevated protein concentrations? > > Any information is greatly appreciated! > > Georg > > -- The address kresten@my-dejanews.com is for spambots only. Please mail me at LysLeuLeu@crc.dk , transforming the pre@-part into my initials. Kresten Lindorff Larsen, Dept. Yeast Genetics Carlsberg Laboratory, Denmark Sent via Deja.com http://www.deja.com/ Share what you know. Learn what you don't. From owner-proteins@net.bio.net Mon Jul 12 03:22:00 1999 Path: biosci!agate!newsfeed.berkeley.edu!dispose.news.demon.net!demon!newsfeed.tli.de!news.algonet.se!newsfeed1.telenordia.se!algonet!newsfeed1.funet.fi!newsfeed.sunet.se!news01.sunet.se!news99.sunet.se!news.chalmers.se!not-for-mail From: Olle Vidal Newsgroups: bionet.molbio.proteins Subject: PTH receptor antibodies Date: Mon, 12 Jul 1999 13:09:40 +0200 Organization: RCEM Message-ID: <3789CCF4.8C92D5BE@medic.gu.se> NNTP-Posting-Host: kkem66.clab.gu.se Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Trace: nyheter.chalmers.se 931778209 6674 130.241.82.43 (12 Jul 1999 11:16:49 GMT) X-Complaints-To: abuse@chalmers.se NNTP-Posting-Date: 12 Jul 1999 11:16:49 GMT X-Mailer: Mozilla 4.5 [en] (WinNT; I) X-Accept-Language: en Lines: 3 I'm looking for antibodies for the PTH receptor. Are there any commercial ones available? From owner-proteins@net.bio.net Tue Jul 13 01:00:00 1999 Path: biosci!internet!biosci!not-for-mail From: biohelp (BIOSCI Administrator) Newsgroups: bionet.molbio.proteins Subject: BIOSCI/bionet miniFAQ & Fundraiser Date: 13 Jul 1999 02:00:12 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 233 Sender: daemon@net.bio.net Distribution: world Message-ID: <199907130900.CAA17743@net.bio.net> NNTP-Posting-Host: net.bio.net (LAST REVISION: 30-JUL-95) This BIOSCI "miniFAQ" is designed to answer the questions that come up the *most frequently*. The main BIOSCI FAQ (Frequently Asked Questions) is accessible on the World Wide Web at URL http://www.bio.net/. If you can not find an answer to your question in this or other documentation, the BIOSCI technical support staff answers e-mail queries sent to biosci-help@net.bio.net We can only answer questions about the use of the newsgroups and mailing lists. We unfortunately do not have the staff to do Internet information searches or answer scientific questions. Please post those to the appropriate BIOSCI/bionet newsgroups. Contents: -------- 0) BIOSCI NEEDS YOUR SUPPORT!! 1) Using the WWW to access the BIOSCI/bionet newsgroups. 2) What to do about "spams," i.e., junk mail, ads, etc. 3) Examples of subscribing and unsubscribing to the mailing lists. 4) The BIOSCI user address and research interest directory. 0) BIOSCI NEEDS YOUR SUPPORT!! ------------------------------ BIOSCI's government funding has been expended, and we are now operating solely from advertising revenue that we have raised from our Web site at http://www.bio.net/. We need just a few minutes of your time to help us serve you. You can do two important things which will take very little time for you individually and will immensely help us continue to help you. First, please use our WWW system at http://www.bio.net/ to access the archives. You can post or reply to messages via your Web browser as described in item #1 below. Your usage helps attract sponsors. If you contact any of our sponsors, please be sure to thank them for supporting BIOSCI. It is critical for them to get this feedback if they are to continue their sponsorship for the long term. Second, if you work for a company or organization that provides products or services of interest to the biology community, please pass this message on to your marketing or marketing communications department or other appropriate group. Please ask them to help support BIOSCI by sponsoring our Web site and explain the uses and benefits of the system to the biology community. If they are interested, they can then contact us for further information at our tech support address, biosci-help@net.bio.net. 1) Using the WWW to access the BIOSCI/bionet newsgroups. -------------------------------------------------------- As of 10 December 1995, all BIOSCI/bionet full newsgroups are accessible through the World Wide Web (WWW) at URL http://www.bio.net. One can read and reply publicly or privately to both recent postings and archived messages through one's Web browser if it is configured properly to send e-mail. Each newsgroup is equipped with its own WAIS index. The main BIOSCI home page also has access to the BIO-JOURNALS Table of Contents database WAIS index and the BIOSCI user address database described in another item further below. 2) What to do about "spams," i.e., junk mail, ads, etc. ------------------------------------------------------- BIOSCI is a set of parallel USENET newsgroups (the "bionet" groups), mailing lists, and a hypermail archive at URL http://www.bio.net/. The same postings are distributed on all media (except for a small number of mailing-list-only groups at net.bio.net). Unfortunately it is becoming a despicable practice on the Internet (by a few people out to make a fast buck) to do automated mass postings to thousands of newsgroups and mailing lists. These attempts to grab free advertising are refered to as "spams" in the usual, somewhat boneheaded, net terminology. USENET is more susceptible to this practice, and many spams originate on the USENET groups and then are passed on to the mailing lists. However, spammers also get lists of mailing addresses and hit these too, so neither medium is immune. What should you do personally if you get junk mail? --------------------------------------------------- Just delete it and move on without reading it further. Filing a protest is becoming increasingly useless because spammers are often disguising the addresses where the messages are sent from. Unless you really understand Internet mail systems, your attempt at protest by sending replies to the message will often end up being sent to the address of an innocent person that the spammer is victimizing. What can BIOSCI/bionet do to protect its newsgroups? ---------------------------------------------------- The only solution currently available is to moderate the newsgroup. If this newsgroup is already moderated, then you are in good shape. Moderation protects the USENET distribution from about 95% of the spams that are being sent to date and protects the mailing lists completely. Moderation means, however, that someone has to take the time to review each message before it goes out. We have set up software here that simply allows the moderator to forward to an address at net.bio.net messages that (s)he wishes to have distributed. This takes no more time than that needed to read the message and pass it on, say about 1 min. per message. Most newsgroups currently have a discussion leader who is responsible for their newsgroup. The discussions leaders and their e-mail addresses are listed in the BIOSCI Information Sheet which is available on the Web at http://www.bio.net/. If a newsgroup is being hit with too many junk postings, please contact the discussion leader for that group and see if there is interest in moderating the group. Please do not assume that by simply posting a complaint to the newsgroup itself, anyone on the BIOSCI staff will act on your complaint. With close to 100 newsgroups to run, the BIOSCI staff has to rely on the discussion leaders of each newsgroup to report problems directly to us at biosci-help@net.bio.net. We will moderate any of our newsgroups if the discussion leader tells us that the readership of the group wishes to do so and if a moderator is willing to do the work. For most BIOSCI/bionet groups, this entails only a few minutes of work each day. Moderating a newsgroup will resolve probably 95% of the junk postings on the USENET distribution. Unfortunately there are easy ways for determined spammers to override the moderation mechanism on USENET, but we can protect our e-mail subscribers from unwanted postings if the newsgroup is moderated. You can also access our newsgroups over the WWW at URL http://www.bio.net. While this Web interface will not stop spammers from trying to post to the groups, this will give you yet another way, besides using USENET news, to keep the junk out of your personal mail files. For those of you with local USENET news systems, the Web interface will also give you faster access to new newsgroups and recent postings. 3) Examples of subscribing and unsubscribing to the mailing lists. ------------------------------------------------------------------ PLEASE NOTE: The BIOSCI management does NOT act on subscription/unsubscription requests that are posted improperly to the newsgroups and mailing lists. People who do this only bother everyone on the lists to no avail. Please be sure to follow the proper procedures below. Gory details are in the BIOSCI Information sheets on the Web at http://www.bio.net. Below we give an example utilizing the METHODS-AND-REAGENTS list at both of our two BIOSCI sites: Users in the Americas and Pacific Rim countries who use the BIOSCI ------------------------------------------------------------------ node at computer net.bio.net: ---------------------------- A) Determine the "listname" which is the <=8 character mail address ^^^^^^^^^^^^^ for the group. These can be found in the BIOSCI Info. Sheet. For the METHODS-AND-REAGENTS group the mailing address is methods@net.bio.net. The listname is the portion of the address to the left of the @ sign, i.e., "methods". The listname is used with the "subscribe" and "unsubscribe" commands illustrated below. B) Mail all commands in the body of a mail message addressed to biosci-server@net.bio.net. Do NOT send commands to the newsgroup posting addresses! Leave the Subject: line blank, any text on it will be ignored. C) In the body of your message put one or more of the following commands with an "end" command on the last line, e.g., subscribe methods unsubscribe methods end Do NOT put your e-mail address or other text on these lines. The server only allows you to cancel your subscription if the address on your mail header matches the address on our mailing list. Please ask for help at biosci-help@net.bio.net if your address has changed, e.g., if you know you are on the list but the server tells you that you are not a member. Users in Europe, Africa, and Central Asia who use the BIOSCI node at -------------------------------------------------------------------- computer daresbury.ac.uk (also known as dl.ac.uk): ------------------------------------------------- To subscribe and unsubscribe to/from the BIOSCI lists, you need to specify the full USENET newsgroup name with "bionet-news." prepended. The USENET newsgroup names are listed in the BIOSCI Information sheet on the Web at http://www.bio.net/. For the METHODS-AND-REAGENTS list the USENET newsgroup name is bionet.molbio.methds-reagnts, thus the appropriate commands are sub bionet-news.bionet.molbio.methds-reagnts unsub bionet-news.bionet.molbio.methds-reagnts These commands are included in a message addressed to mxt@dl.ac.uk, NOT to the newsgroup mailing addresses. As usual, include the text in the body of the message as text on the Subject: line is ignored. To unsubscribe from all the lists at the UK node, use unsub bionet-news Please note that if the address in the list is different than the one in your mail message header, you will not be able to unsubscribe by this method. If you have problems, please mail biosci@daresbury.ac.uk. 4) The BIOSCI user address and research interest directory. ----------------------------------------------------------- Please take this opportunity to add your name, address, and research interest information to the BIOSCI User Address Database if you have not already done so. You can fill out the address form directly through our Web page at URL http://www.bio.net/adrform.html. The address database is reindexed nightly for WWW access (the URL is http://www.bio.net/). If you are not directly on the Internet but can reach it by e-mail, please use our waismail server to access the user directory. waismail use is described above. You can also request a user address form by e-mail from biosci-help@net.bio.net. Please check your database entry from time-to-time to see if your address information is still up-to-date. Because of our limited personnel resources, we ask that you resubmit a *complete* form to revise your entry; we only replace complete entries and do not have resources to edit old forms. From owner-proteins@net.bio.net Tue Jul 13 01:51:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.concentric.net!newshub.northeast.verio.net!news.maxwell.syr.edu!easynet-tele!easynet.net!server5.netnews.ja.net!keele!news From: "Matthew Peake" Newsgroups: bionet.molbio.proteins Subject: sourcing RGD peptides, please help. Date: Tue, 13 Jul 1999 10:16:27 +0100 Lines: 14 Distribution: world Message-ID: <7mf03c$sh1$1@cfs2.kis.keele.ac.uk> NNTP-Posting-Host: mpc12.pmed.keele.ac.uk X-Priority: 3 X-MSMail-Priority: Normal X-Newsreader: Microsoft Outlook Express 5.00.2314.1300 X-MimeOLE: Produced By Microsoft MimeOLE V5.00.2314.1300 I am trying to find a source of RGD peptides for cell adhesion studies. I particular GRGDS or GRGDNP peptides for blocking RGD mediated adhesion. I have previously used those produced by SIGMA (product numbers G 2529 or G 4391) but they have just stopped supplying them. If anyone could suggest a different source for a similar price (i.e. about 70 to 80 pounds sterling for five milligrams) I would be very grateful. Thanks in advance, Matthew Peake From owner-proteins@net.bio.net Tue Jul 13 02:51:00 1999 From: Jens Lohrmann Newsgroups: bionet.molbio.proteins Subject: Phosphoramidate Date: Tue, 13 Jul 1999 11:01:38 +0200 Organization: Rechenzentrum der Universitaet Freiburg, Germany Lines: 57 Message-ID: <378B0071.4D7CE6E6@sun2.ruf.uni-freiburg.de> NNTP-Posting-Host: tomate.biologie.uni-freiburg.de Mime-Version: 1.0 Content-Type: multipart/mixed; boundary="------------B97AE6967DC3BDD966B2955C" X-Mailer: Mozilla 4.5 [de] (Win95; I) X-Accept-Language: de Path: biosci!news.stanford.edu!newsfeed.stanford.edu!nntp.cs.ubc.ca!news-spur1.maxwell.syr.edu!news.maxwell.syr.edu!tank.news.pipex.net!pipex!newsfeed.nacamar.de!newsfeed.nacamar.de!rz.uni-karlsruhe.de!news.uni-ulm.de!news.belwue.de!news.uni-freiburg.de!not-for-mail Dies ist eine mehrteilige Nachricht im MIME-Format. --------------B97AE6967DC3BDD966B2955C Content-Type: text/plain; charset=iso-8859-1 Content-Transfer-Encoding: 8bit Dear Netters! I’m looking for some information about phosphoramidate. I’m working in a molecular plant physiology lab and would like to run an experiment using p32-labelled phosphoramidate. Unfortunately I’m not aware of a commercial supplier selling the labelled reagent or an unlabelled precursor. So please kindly inform me if you know about a company selling either the p32-labelled phosphoramidate or the precursor. The second question would be the following: does someone know a lab or work in a lab which is synthesising phosphoramidate or the precursor in a non-commercial scale and is willing to share an aliquot? I greatly appreciate your help and really look desperately forward to your answer! Jens Lohrmann Albert-Ludwigs-University Freiburg, Germany lohrmann@sun2.ruf.uni-freiburg.de --------------B97AE6967DC3BDD966B2955C Content-Type: text/x-vcard; charset=us-ascii; name="lohrmann.vcf" Content-Transfer-Encoding: 7bit Content-Description: Visitenkarte für Jens Lohrmann Content-Disposition: attachment; filename="lohrmann.vcf" begin:vcard n:Lohrmann;Jens tel;pager:ich bin tel;cell:doch so tel;fax:unwichtig!!!!!! tel;home:0761/402351 tel;work:0761/293-2619 x-mozilla-html:TRUE adr:;;;;;; version:2.1 email;internet:lohrmann@sun2.ruf.uni-freiburg.de title:Dipl. note:ich hab Euch lieb!!! fn:Jens Lohrmann end:vcard --------------B97AE6967DC3BDD966B2955C-- From owner-proteins@net.bio.net Tue Jul 13 04:17:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!cgl!itssrv1.ucsf.edu!usenet From: "Long" Newsgroups: bionet.molbio.proteins Subject: Protocol site Date: Mon, 12 Jul 1999 20:20:50 -0700 Organization: UCSF, ITS Lines: 21 Message-ID: <7meb2g$1v3e@itssrv1.ucsf.edu> NNTP-Posting-Host: shiva-lr25-1.ucsf.edu X-Priority: 3 X-MSMail-Priority: Normal X-Newsreader: Microsoft Outlook Express 5.00.2314.1300 X-MimeOLE: Produced By Microsoft MimeOLE V5.00.2314.1300 Dear Researcher, If you need a protocol, visit http://biousa.hypermart.net This site has a comprehensive collection of well categorized molecular biology protocols. All of them are just a click away. If you got some problem with your experiment, come in and join the discussion forum http://biousa.hypermart.net/discussion to post your question or provide answer to other's question. All articles are searchable. Enjoy Long begin 666 Me.vcf M0D5'24XZ5D-!4D0-"E9%4E-)3TXZ,BXQ#0I..CM,;VYG#0I&3CI-90T*14U! M24P[4%)%1CM)3E1%4DY%5#IL:6QC-SE >6%H;V\N8V]M#0I2158Z,3DY.3 W 7,3-4,#,R,#4P6@T*14Y$.E9#05)$#0H` ` end From owner-proteins@net.bio.net Wed Jul 14 11:36:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!headwall.stanford.edu!HSNX.callatg.com!nuq-feed.news.verio.net!feed.news.verio.net!nuq-peer.news.verio.net!nntp.primenet.com!nntp.gctr.net!newspeer1.nac.net!news.maxwell.syr.edu!nntp2.deja.com!nnrp1.deja.com!not-for-mail From: mujwal@rics.bwh.harvard.edu Newsgroups: bionet.molbio.proteins Subject: Detection of Heme in Membrane Proteins Date: Wed, 14 Jul 1999 19:16:56 GMT Organization: Deja.com - Share what you know. Learn what you don't. Lines: 19 Message-ID: <7minmr$peh$1@nnrp1.deja.com> NNTP-Posting-Host: 134.174.176.37 X-Article-Creation-Date: Wed Jul 14 19:16:56 1999 GMT X-Http-User-Agent: Mozilla/4.06 [en] (Win95; I) X-Http-Proxy: 1.0 x27.deja.com:80 (Squid/1.1.22) for client 134.174.176.37 I am wondering, if anyone would suggest/advice any method to detect heme in an integral membrane protein. The amino acid sequence has a typical CXXCH motif common among several heme proteins. The protein is expressed in a heterologous system, but not purified. Assay system reports the high activity in the heterologous system. As mentioned, purification protocols have not been established. Is there some kind of in-situ staining for heme proteins. Sincerely UJWAL Sent via Deja.com http://www.deja.com/ Share what you know. Learn what you don't. From owner-proteins@net.bio.net Thu Jul 15 01:46:00 1999 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!newsfeed.icl.net!ayres.ftech.net!news.ftech.net!easynet-tele!easynet.net!server5.netnews.ja.net!server6.netnews.ja.net!nntphost.dur.ac.uk!not-for-mail From: "Lee.Hunt" Newsgroups: bionet.molbio.proteins Subject: Re: Electro-elution Date: Thu, 15 Jul 1999 10:40:16 +0100 Organization: University of Durham, Durham, UK. Lines: 19 Message-ID: <378DAC80.1198D51E@durham.ac.uk> References: <3784C7B7.210478C7@dds.nl> NNTP-Posting-Host: biosci01.dur.ac.uk Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 4.61 [en] (WinNT; I) X-Accept-Language: en Do you want to retain activity? We use Schleicher and Schuells Biotrap to purify denatured proteins for antibody work. This can concentrate the sample also, so from a full mini gel the final volume will be about 100 microlitres Martijn van Duijn wrote: > > Hi, > > Does anyone know a good protocol for the electro-elution of a protein > (30 kD) from excised bands of a polyacrylamide gel? I would like to pool > the bands from all slots of a gel, and then concentrate the protein in > it for further analysis. > The protein I am interested in is an integral membrane protein, in case > this causes special problems I should be aware of. > > Thanks for helping me out! > > Martijn From owner-proteins@net.bio.net Thu Jul 15 22:45:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!news-peer1.sprintlink.net!news-in-central.sprintlink.net!news.sprintlink.net!news.wa-k20.net!news.wsu.edu!cheetah!kwon1 From: Young Ho Kwon Newsgroups: bionet.molbio.proteins Subject: Re: Phosphoramidate Date: Thu, 15 Jul 1999 22:46:09 -0700 Organization: Washington State University Lines: 33 Message-ID: References: <378B0071.4D7CE6E6@sun2.ruf.uni-freiburg.de> NNTP-Posting-Host: cheetah.it.wsu.edu Mime-Version: 1.0 Content-Type: TEXT/PLAIN; charset=US-ASCII Content-Transfer-Encoding: QUOTED-PRINTABLE X-Sender: kwon1@cheetah In-Reply-To: <378B0071.4D7CE6E6@sun2.ruf.uni-freiburg.de> Glen Research may have some information about that. Tel) 1-800-327-4536 On Tue, 13 Jul 1999, Jens Lohrmann wrote: > Dear Netters! >=20 > I=92m looking for some information about phosphoramidate. I=92m working i= n a >=20 > molecular plant physiology lab and would like to run an experiment using >=20 > p32-labelled phosphoramidate. Unfortunately I=92m not aware of a > commercial supplier selling the labelled reagent or an unlabelled > precursor. >=20 > So please kindly inform me if you know about a company selling either > the p32-labelled phosphoramidate or the precursor. >=20 > The second question would be the following: does someone know a lab or > work in a lab which is synthesising phosphoramidate or the precursor in > a non-commercial scale and is willing to share an aliquot? >=20 > I greatly appreciate your help and really look desperately forward to > your answer! >=20 > Jens Lohrmann > Albert-Ludwigs-University > Freiburg, Germany >=20 > lohrmann@sun2.ruf.uni-freiburg.de >=20 From owner-proteins@net.bio.net Fri Jul 16 06:59:00 1999 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!dispose.news.demon.net!demon!news.maxwell.syr.edu!newsfeed.cwix.com!152.163.199.19!portc03.blue.aol.com!audrey03.news.aol.com!not-for-mail From: stcaris@aol.com (Stcaris) Newsgroups: bionet.molbio.proteins Subject: Anti-PEG antibodies? NNTP-Posting-Host: ladder06.news.aol.com X-Admin: news@aol.com Date: 16 Jul 1999 14:53:25 GMT Organization: AOL Bertelsmann Online GmbH & Co. KG http://www.germany.aol.com Message-ID: <19990716105325.18204.00001051@ng-fj1.aol.com> Lines: 30 Dr. R. Flaig c/o Prof. G. Fricker Institute for Pharmaceutical Technology, University of Heidelberg INF 366, D-69120 Heidelberg Ladies and gentlemen, we are currently in search of an antibody directed against polyethylene glycol (PEG) for the purpose of detecting and tracing PEG-coated liposomes ("stealth liposomes") and would like to hear about anybody who has such ABs (first described by Richter & Akerblom in 1983). If such antibodies are not available, we would be grateful for any further information on this subject. Expecting your answer, R. Flaig === Yours sincerely, Chevalier Dr. Ruediger Marcus Flaig Email: sanctacaris@bigfoot.com sanctacaris@unforgettable.com sanctacaris@rocketmail.com sanctacaris@hotmail.com stcaris@aol.com 01727652946@d2-message.de (mobile - short mails only) "Tell truth and shame the devil." (Shakespeare, Henry IV.) From owner-proteins@net.bio.net Sun Jul 18 15:26:00 1999 Path: biosci!newshost.lanl.gov!awabi.library.ucla.edu!128.230.129.106!news.maxwell.syr.edu!howland.erols.net!dispose.news.demon.net!demon!news-lond.gip.net!news.gsl.net!gip.net!tank.news.pipex.net!pipex!newsfeed.amsterdam.nl.net!sun4nl!xs4all!not-for-mail From: "Michael 'Muscular' Sleurink" Newsgroups: sci.med.nutrition,bionet.molbio.proteins,alt.support.diet.low-carb,alt.support.diet.low-fat Subject: Re: Excess proteins in diet Date: Mon, 19 Jul 1999 01:22:34 +0200 Organization: XS4ALL Internet BV Message-ID: <7mtnfm$ade$1@news1.xs4all.nl> References: <3785eda4.4025022@news3.webzone.net> <7m3234$rl4$1@oak.prod.itd.earthlink.net> <378a523a.5742531@news.gte.net> NNTP-Posting-Host: dc2-isdn1039.dial.xs4all.nl X-Trace: news1.xs4all.nl 932340022 10670 194.109.152.15 (18 Jul 1999 23:20:22 GMT) X-Complaints-To: abuse@xs4all.nl NNTP-Posting-Date: 18 Jul 1999 23:20:22 GMT X-Priority: 3 X-MSMail-Priority: Normal X-Newsreader: Microsoft Outlook Express 5.00.2314.1300 X-MimeOLE: Produced By Microsoft MimeOLE V5.00.2314.1300 Lines: 14 I think you are joking. But this is the real thing. Answer on question number 1: when protein comes in the stomach, it will be taken to the liver. The liver splits up the protein in aminoacids. There are alot of aminoacids, like Asparatic Acid, Glutamic Acid, Lysine, Valine, Isoleucine, etc. But each amino acid has a specific funtion. E.g. : Glutamic Acid helps repairing wounds. But when there's no Glutamic Acide available from the liver, it will be taken out from the muscles, and that is what bodybuilders are trying to prevent. So what do they, they take some more Glutamic Acid From owner-proteins@net.bio.net Sun Jul 18 15:59:00 1999 Path: biosci!agate!newsfeed.berkeley.edu!dispose.news.demon.net!demon!feed1.news.rcn.net!rcn!howland.erols.net!portc02.blue.aol.com!pitt.edu!not-for-mail From: pxpst2@vms.cis.pitt.edu (Peter) Newsgroups: sci.med.nutrition,bionet.molbio.proteins,alt.support.diet.low-carb,alt.support.diet.low-fat Subject: Re: Excess proteins in diet Date: Sun, 18 Jul 1999 19:51:44 -0400 Organization: University Of Pittsburgh Message-ID: References: <3785eda4.4025022@news3.webzone.net> <7m3234$rl4$1@oak.prod.itd.earthlink.net> <378a523a.5742531@news.gte.net> <7mtnfm$ade$1@news1.xs4all.nl> NNTP-Posting-Host: pelli.pathology.pitt.edu Mail-Copies-To: pxpst2@vms.cis.pitt.edu X-Newsreader: MT-NewsWatcher 2.4.4 Lines: 51 In article <7mtnfm$ade$1@news1.xs4all.nl>, "Michael 'Muscular' Sleurink" wrote: > Answer on question number 1: > when protein comes in the stomach, it will be taken to the liver. The liver > splits up the protein in aminoacids. There are alot of aminoacids, like > Asparatic Acid, Glutamic Acid, Lysine, Valine, Isoleucine, etc. But each > amino acid has a specific funtion. > E.g. : Glutamic Acid helps repairing wounds. But when there's no Glutamic > Acide available from the liver, it will be taken out from the muscles, and > that is what bodybuilders are trying to prevent. So what do they, they take > some more Glutamic Acid If this is a joke...HAHAHAHAHAHA This is not how digestion and adsorption works. Maybe this is the Marvel Comic version but it is not right. Although some amino acids are needed for specialty functions like the creation of neurotransmiters, they are all needed. In large part, the body must get a uniform distribution of all the aa's for its various functions namely building other proteins that do specilized tasks. A muscle cell will not catabolize itself for nutrients because it is not equiped to do so. The enzymes needed are not there. As for what body builders do, They are largely idiots that go on a grain of truth and without really knowing what they are doing. I am by no means saying that all body builders are idiots but many are. For example, the last craze that I remeber that was popularized by Mark Mcguire and it involved the administration of androstendione thinking that it is converted to testosterone. It is not rather it is converted to estrogen. So they wanted big pectorals, they got big mammeries. Could you please tell me your source for the info that glutamic acid facilitates the repairing of wounds? With my extensive knowledge in various wound repairs, from bone to skin, I have never heard this. The only thing special about glutamic acid is that coagulation protiens are often gamma carboxylated on them to facilitate sticking to negatively charged surfaces such as cell membranes or basement matrix. The only amaino acids that would in any remote way facilitate the repair of skin and other tissues, would be the ones that are needed to synthesize collagen. -- Peter _____________________________________________________________________ " Some of you might not agree 'Cause you probably likes a lot of misery But think a while and you will see... Broken hearts are for assholes" FZ From owner-proteins@net.bio.net Sun Jul 18 16:21:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!news.maxwell.syr.edu!newsfeed.wirehub.nl!xs4all!not-for-mail From: "Michael 'Muscular' Sleurink" Newsgroups: sci.med.nutrition,bionet.molbio.proteins,alt.support.diet.low-carb,alt.support.diet.low-fat Subject: Re: Excess proteins in diet Date: Mon, 19 Jul 1999 02:17:30 +0200 Organization: XS4ALL Internet BV Lines: 68 Message-ID: <7mtqmm$d2v$1@news1.xs4all.nl> References: <3785eda4.4025022@news3.webzone.net> <7m3234$rl4$1@oak.prod.itd.earthlink.net> <378a523a.5742531@news.gte.net> <7mtnfm$ade$1@news1.xs4all.nl> NNTP-Posting-Host: dc2-isdn1057.dial.xs4all.nl X-Trace: news1.xs4all.nl 932343318 13407 194.109.152.33 (19 Jul 1999 00:15:18 GMT) X-Complaints-To: abuse@xs4all.nl NNTP-Posting-Date: 19 Jul 1999 00:15:18 GMT X-Priority: 3 X-MSMail-Priority: Normal X-Newsreader: Microsoft Outlook Express 5.00.2314.1300 X-Mimeole: Produced By Microsoft MimeOLE V5.00.2314.1300 I got it from my fitness magazine. But what you say is not true, I think. Cells of muscle can be catabolized with the hormone cortison, I thought. Example: when a person goes on a diet that contains only carbohydrates and fat, he will be needed aminoacids for several bosyfunctions. Think of woundhealing, I thought making of body hormones. Reactions plz. Peter schreef in berichtnieuws pxpst2-1807991951450001@pelli.pathology.pitt.edu... > In article <7mtnfm$ade$1@news1.xs4all.nl>, "Michael 'Muscular' Sleurink" > wrote: > > > Answer on question number 1: > > when protein comes in the stomach, it will be taken to the liver. The liver > > splits up the protein in aminoacids. There are alot of aminoacids, like > > Asparatic Acid, Glutamic Acid, Lysine, Valine, Isoleucine, etc. But each > > amino acid has a specific funtion. > > E.g. : Glutamic Acid helps repairing wounds. But when there's no Glutamic > > Acide available from the liver, it will be taken out from the muscles, and > > that is what bodybuilders are trying to prevent. So what do they, they take > > some more Glutamic Acid > > If this is a joke...HAHAHAHAHAHA > > This is not how digestion and adsorption works. Maybe this is the Marvel > Comic version but it is not right. > > Although some amino acids are needed for specialty functions like the > creation of neurotransmiters, they are all needed. In large part, the > body must get a uniform distribution of all the aa's for its various > functions namely building other proteins that do specilized tasks. > A muscle cell will not catabolize itself for nutrients because it is not > equiped to do so. The enzymes needed are not there. As for what body > builders do, They are largely idiots that go on a grain of truth and > without really knowing what they are doing. I am by no means saying that > all body builders are idiots but many are. For example, the last craze > that I remeber that was popularized by Mark Mcguire and it involved the > administration of androstendione thinking that it is converted to > testosterone. It is not rather it is converted to estrogen. So they > wanted big pectorals, they got big mammeries. > > Could you please tell me your source for the info that glutamic acid > facilitates the repairing of wounds? With my extensive knowledge in > various wound repairs, from bone to skin, I have never heard this. The > only thing special about glutamic acid is that coagulation protiens are > often gamma carboxylated on them to facilitate sticking to negatively > charged surfaces such as cell membranes or basement matrix. The only > amaino acids that would in any remote way facilitate the repair of skin > and other tissues, would be the ones that are needed to synthesize > collagen. > > -- > Peter > > _____________________________________________________________________ > " Some of you might not agree > 'Cause you probably likes a lot of misery > But think a while and you will see... > Broken hearts are for assholes" > FZ From owner-proteins@net.bio.net Mon Jul 19 06:49:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!sunqbc.risq.qc.ca!newsflash.concordia.ca!pitt.edu!not-for-mail From: pxpst2@vms.cis.pitt.edu (Peter) Newsgroups: sci.med.nutrition,bionet.molbio.proteins,alt.support.diet.low-carb,alt.support.diet.low-fat Subject: Re: Excess proteins in diet Date: Mon, 19 Jul 1999 10:42:19 -0400 Organization: University Of Pittsburgh Lines: 65 Message-ID: References: <3785eda4.4025022@news3.webzone.net> <7m3234$rl4$1@oak.prod.itd.earthlink.net> <378a523a.5742531@news.gte.net> <7mtnfm$ade$1@news1.xs4all.nl> <7mtqmm$d2v$1@news1.xs4all.nl> NNTP-Posting-Host: pelli.pathology.pitt.edu Mail-Copies-To: pxpst2@vms.cis.pitt.edu X-Newsreader: MT-NewsWatcher 2.4.4 In article <7mtqmm$d2v$1@news1.xs4all.nl>, "Michael 'Muscular' Sleurink" wrote: > I got it from my fitness magazine. But what you say is not true, I think. > Cells of muscle can be catabolized with the hormone cortison, I thought. Cortisol/cortisone and others are member of a family of hormones which are ligands for the glucocorticoid receptor. They are all derived from choloesterol and since they are transcription factors, they act to turn on or turn off production a certain proteins. They act differently in different tissues. The general effect of these hormones is to maintain glucose production from protein (catabolic action in muscle, see below),facilitate fat metabolism, supports vascular responsivness and modulates CNS function. This is a very general list and within different tissues or with different cells other action may be seen. For example cortisone can act to inhibit the inflametory response if given in one area. With regard to muscle, Cortisol has a dual action. 1) In absence of of hormone, the contractility and work ability of the muscle cell declines. The action of cortisol in low doses on skelatal muscle is thought to be exerted at the Myoneural junction (point where nerve meets muscle fiber) which acts to increase the acetylcholibe synethesis. With regard to cardiac muscle Cortisol is thought to increase the number of beta adrenergic receptors. 2) When excess cortisol is present, the action of cortisol is to divert aa's from the production of proteins to the production of glucose to form energy. This I would believe is what you are refering to as catabolic action. But this is not a normal action, this is a side effect of cortisol administration as a drug. But the muscle cells do not die they just stop working due to the fact that proteins involved in a stress response are being upregulated to make energy and they may do it at the expense of making proteins needed for muscle function. Amino acids that would have been used to make proteins are converted to glucose to make energy. When the muscle cells die from necrossis, they are not taken up by neighboring muscle cells rather the infiltrating leukocytes/phagocytes come in and clean up. > Example: when a person goes on a diet that contains only carbohydrates and > fat, he will be needed aminoacids for several bosyfunctions. Think of > woundhealing, I thought making of body hormones. amino acids can be broken into two catagories essential aa's which are incabable of being made by the body and non essential which can be made by the body. All 20 aa's must be present for normal protein production. If one is lacking then protein production is impaired. With regard to wound healing, it is a complicated process that involves specialized cells and has little to do with any particular aa. The only reason aa's are needed is to make proteins to support the specialized cells that are involved in the repair. If you want to more info on wound healing then tell me a specific tissue and I will give you a good refernce for learning more. Also, be careful with the term hormone. Is is a slipery word. With regard to the skin, the action of wound healing is stimulated by EGF(whichis thought to be stored in the matrix and released upon injury) which is not a classical hormne rather a growth factor. Regards Peter Pediaditakis Dept. of Pathology University of Pittsburgh From owner-proteins@net.bio.net Mon Jul 19 10:27:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!remarQ73!supernews.com!remarQ.com!remarQ69!WReNclone!WReNphoon4.POSTED!WReN!not-for-mail From: laughingdragon Newsgroups: sci.med.nutrition,bionet.molbio.proteins,alt.support.diet.low-carb,alt.support.diet.low-fat Subject: Re: Excess proteins in diet Organization: http://www.remarq.com: The World's Usenet/Discussions Start Here X-Originating-Host: 162.119.232.100 X-Wren-Trace: cJC3l4KQzLSM3sSygNzRyNvD0cTPxoDcxcXfwsDd0JDOwILfz4Hc0M7CxtvPgNPHkJCYjY7LoJ2xhtWKl56Hl5g= Message-ID: <932408409.1987@www.remarq.com> References: <3785eda4.4025022@news3.webzone.net> <7m3234$rl4$1@oak.prod.itd.earthlink.net> <378a523a.5742531@news.gte.net> <7mtnfm$ade$1@news1.xs4all.nl> <7mtqmm$d2v$1@news1.xs4all.nl> Lines: 42 Date: Mon, 19 Jul 1999 10:20:05 -0800 NNTP-Posting-Host: 10.0.3.195 X-Complaints-To: wrenabuse@remarq.com X-Trace: WReNphoon4 932408295 10.0.3.195 (Mon, 19 Jul 1999 11:18:15 PDT) NNTP-Posting-Date: Mon, 19 Jul 1999 11:18:15 PDT Oops...here's a new one. Hemochromatosis. I just read an article on it. It's a syndrome of excess absorption of iron from the diet. Primarily from meat. My dad just got a diagnosis of it a couple of weeks ago so when I saw the article, I decided to read it. Hemochromatosis: A Common, Rarely Diagnosed Disease By Vincent J. Felitti, MD, FACP Commentary by David Baer, MD, FACP These guys say 30,000 have it, 1000 have been diagnosed. That's for the homozygous variety. Heterozygous state is 1 in 250 people. In Ireland homozygous state is 1 in 80! The hypothesis is that the mutation first occurred in Ireland. So, what does that mean? For me and my family it explains the onset of adult diabetes, odd liver tests, possibly one case of chronic heart failure and perhaps hypothyroidism. Darn, I just went on a low carb diet after ten years of near vegetarianism. Before that I had done low carb for years. The only good thing is that this time I really don't have that much of an appetite. But I have a feeling I'd better get a check on my ferritin levels. Just a warning folks. Yours, Jackie Sent from RemarQ http://www.remarq.com/?z The Internet's Discussion Network The fastest and easiest way to search and participate in Usenet - Free! From owner-proteins@net.bio.net Mon Jul 19 10:42:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!remarQ73!supernews.com!remarQ.com!remarQ69!WReNclone!WReNphoon4.POSTED!WReN!not-for-mail From: laughingdragon Newsgroups: sci.med.nutrition,bionet.molbio.proteins,alt.support.diet.low-carb,alt.support.diet.low-fat Subject: Re: Excess proteins in diet Organization: http://www.remarq.com: The World's Usenet/Discussions Start Here X-Originating-Host: 162.119.232.100 X-Wren-Trace: cDAXNyIwbBQsfmQSIHxxaHtjcWRvZyV8Zm9/YmB9cDBuYCJ/byF8cG5iZntvIHNnMDA4LS5rAD0RJnUqNz4nNzg= Message-ID: <932409333.2185@www.remarq.com> References: <3785eda4.4025022@news3.webzone.net> <7m3234$rl4$1@oak.prod.itd.earthlink.net> <378a523a.5742531@news.gte.net> <7mtnfm$ade$1@news1.xs4all.nl> <7mtqmm$d2v$1@news1.xs4all.nl> <932408409.1987@www.remarq.com> Lines: 36 Date: Mon, 19 Jul 1999 10:35:30 -0800 NNTP-Posting-Host: 10.0.3.195 X-Complaints-To: wrenabuse@remarq.com X-Trace: WReNphoon4 932409219 10.0.3.195 (Mon, 19 Jul 1999 11:33:39 PDT) NNTP-Posting-Date: Mon, 19 Jul 1999 11:33:39 PDT Addendum to my other message. I'd taken the wrong statistics on prevalence. 1:8 people carries one gene. 1:64 marriages will be of two people carrying one gene each. 1:4 of the children of those marriages will have two genes for the disorder and will be symptomatic at some stage of their life. That means one person in 250 is homozygous. Or approximately (given 250 million people in the US) one million people in the US have hemochromatosis and will have some or all of it's symptoms. Why isn't it noticed. Because most people haven't seriously toxed themselves until they are old. But, as I've said, too much meat..... The article recommends a $2 test called a transferrin saturation test. (That's the lab's lowest cost, not what you will pay for it). It recommends this test for people at 18, whether or not they are going on diets. The article says this will miss some people with rapid progressive disease but catch most of the rest. Yours, Jackie Sent from RemarQ http://www.remarq.com/?z The Internet's Discussion Network The fastest and easiest way to search and participate in Usenet - Free! From owner-proteins@net.bio.net Mon Jul 19 11:34:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!news-feed.inet.tele.dk!bofh.vszbr.cz!news.algonet.se!algonet!news.tvd.be!uunet!ams.uu.net!News.Amsterdam.UnisourceCS!newsfeed-zh.ip-plus.net!news.ip-plus.net!news.access.ch!not-for-mail From: Stephan Kolb Newsgroups: bionet.molbio.proteins Subject: Who are the protein producers? Date: Mon, 19 Jul 1999 21:28:58 +0200 Organization: nexcom Lines: 11 Message-ID: <37937C7A.E010D6A6@pop.dplanet.ch> Reply-To: nexcom@dplanet.ch NNTP-Posting-Host: dialup-40-59.dplanet.ch Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Trace: pacifica.access.ch 932412523 6387 212.35.40.59 (19 Jul 1999 19:28:43 GMT) X-Complaints-To: newsmaster@access.ch NNTP-Posting-Date: 19 Jul 1999 19:28:43 GMT X-Mailer: Mozilla 4.5 [en]C-CCK-MCD {dplanet-1.0} (Win98; I) X-Accept-Language: en-US,en,fr-FR,es,es-MX Hello Friends, I'm doing a research on the producers of proteins like Boehringer Mannheim, but there are I'm sure many more! If somebody could give me some list or existing database I would be very grateful. Thanks, Stephan Kolb University of Geneva, Switzerland From owner-proteins@net.bio.net Mon Jul 19 16:26:00 1999 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!newsswitch.lcs.mit.edu!news-spur1.maxwell.syr.edu!news.maxwell.syr.edu!feeder.qis.net!newsfeed1.earthlink.net!nntp.earthlink.net!posted-from-earthlink!not-for-mail From: John Philo <"jphilo*NO SPAM12*"@earthlink.net> Newsgroups: bionet.molbio.proteins Subject: Re: Who are the protein producers? Date: Mon, 19 Jul 1999 17:12:15 -0700 Content-Transfer-Encoding: 7bit References: <37937C7A.E010D6A6@pop.dplanet.ch> To: nexcom@dplanet.ch X-Posted-Path-Was: not-for-mail Content-Type: text/plain; charset=us-ascii X-ELN-Date: 20 Jul 1999 00:12:35 GMT X-ELN-Insert-Date: Mon Jul 19 17:15:07 1999 Organization: Alliance Protein Laboratories Lines: 21 Mime-Version: 1.0 NNTP-Posting-Host: 1cust7.tnt2.thousand-oaks.ca.da.uu.net Message-ID: <3793BEDF.D672D233@earthlink.net> X-Mailer: Mozilla 4.05 [en] (Win95; U) The July 5 issue of The Scientist has a huge list of companies producing protein reagents related to cell signaling. And if I remember correctly, a recent issue (within the last month or so) of Genetic Engineering News had a list of companies making cytokines. John Philo Alliance Protein Laboratories Stephan Kolb wrote: > > Hello Friends, > > I'm doing a research on the producers of proteins like Boehringer > Mannheim, but there are I'm sure many more! > If somebody could give me some list or existing database I would be very > grateful. > > Thanks, > > Stephan Kolb > University of Geneva, Switzerland From owner-proteins@net.bio.net Tue Jul 20 03:36:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!logbridge.uoregon.edu!newsfeed.icl.net!newsfeed1.news.nl.uu.net!sun4nl!surfnet.nl!news.nki.nl!not-for-mail From: Annet Grummels Newsgroups: bionet.molbio.proteins Subject: ELISA background Date: Tue, 20 Jul 1999 13:25:57 +0200 Organization