Reduced Protein Gel Behavior

Martin Offterdinger a8803349.nospam at unet.univie.ac.at
Fri Jul 10 03:56:04 EST 1998


On Thu, 09 Jul 1998 17:26:42 -0500, sg at nwu.edu (Stephen Gately) wrote:

>I have a protein that migrates as a doublet at approximately 52 kD on
>denaturing/non-reducing gels.  If I run the sample reduced (BME) the
>protein still runs as a doublet, but the molecular mass increases to 60-64
>kD.
>
>Any thoughts on this occurence?
>
>Thanks,
>
>Steve
Steve!

 1) I think that you are having a protein with an intenal  S-S bond,
that leads to intenal loop formation thus "shortening " the unreduced
protein. If you reduce the protein the loop is destroyed and you see
the full length.
2) The double band should be independent of this phenomenon and may
have various reasons. Partial degradation, differential
phosphorylation , glycosylation,....
Hope this is of some help!
Martin
Martin Offterdinger
Internal Med.I,Dept. Oncology
University of Vienna
Austria
E-Mail:a8803349.nospam at unet.univie.ac.at
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