WILSON at edv1.boku.ac.at
Fri May 5 04:22:22 EST 1995
> Date: 4 May 1995 13:33:44 GMT
> From: srps at galactose.mc.duke.edu (Steven Pirie-Shepherd)
> Reply-to: srps at galactose.mc.duke.edu (Steven Pirie-Shepherd)
> To: "bionet.glycosci mail newsgroup" <bionet-news at dl.ac.uk>
> Subject: Re: protein standards
> Aida Cancel (axc19 at psu.edu) wrote:
> : If you would have to pick two
> : proteins, a glycosylated control and a non-glycosylated control, which
> : ones would you think I should use?
> : Your help will be appreciated,
> Glycosylated control: Fetuin from Gibco BRL or Boehringer Mannheim.
> Non-glycosylate control: some cheap E coli or prokaryote protein or
> recombinant protein would work fine. Bacteria don't have glyco machinary.
This is not necessarily true. Some bacteria do have glycosylated
proteins, although E. coli is not apparently one of them.
Evidence for the covalent linkage of carbohydrate polymers to a
glycoprotein from Streptococcus sanguis
Erickson, PR, and Herzberg, MC (1993) J. Biol. Chem. 268:23780-23783
> What about some old Restriction enzyme lying around the lab?
Thus restriction enzymes from unusual sources may be glycosylated -
one cannot say.
As for the other contributions to this thread - i.e. re: BSA - I
believe that non-enzymatic glycosylation of BSA is possible with
diabetic patients. But I have no refs. on that. And, of course, using
cytoplasmic or nuclear proteins is no guarantee of a
non-glycosylated status, due to the possible presence of O-linked
One thought - isn't mature ConA non-glycosylated?
Iain Wilson Institut fuer Chemie
Tel: 43-1-47654-6065 Universitaet fuer Bodenkultur
Fax: 43-1-310-5176 Gregor-Mendel-Strasse 33
E-mail: wilson at edv1.boku.ac.at A-1180, WIEN, Austria
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