My suggestion below of glycosylation was nonsense. I misread the message
and thought we were talking mass, not IEF mobility.
Ken
Kenneth A. Walsh
E.W.Davie/ZymoGenetics Chair of Biochemistry
Box # 357350
University of Washington
Seattle WA 98195
walsh@u.washington.edu
Phone 206-543-1768
FAX 206-685-9231
---------- Forwarded message ----------
Date: Tue, 28 Jul 1998 15:08:07 -0700 (PDT)
From: Ken Walsh <walsh@u.washington.edu>
To: Kenneth Williams <Kenneth.Williams@yale.edu>
Cc: Recipients of ABRF List <abrf@aecom.yu.edu>
Subject: Re: Posttranslational Modifications
Ken
An interesting possibility for a PTM would be attachment of a single
hexosamine (+161). Gerald Hart has found that specific glycation (with
GlcNac I think) acts to limit phosphorylation.
Ken
Kenneth A. Walsh
E.W.Davie/ZymoGenetics Chair of Biochemistry
Box # 357350
University of Washington
Seattle WA 98195
walsh@u.washington.edu
Phone 206-543-1768
FAX 206-685-9231
On Mon, 27 Jul 1998, Kenneth Williams wrote:
> One of our users is working with a kinase that is phosphorylated at a
> single site. In addition, however, the non-phosphorylated (and
> dephosphorylated) kinase migrates as a doublet on isoelectric focussing -
> with the distance between the two (non-phosphorylated) species being about
> twice the distance between the phospho and non-phosho forms of either
> individual species. My question is what are the most likely
> post-translational modifications that might give rise to the original
> doublet (assuming one species in not modified and that neiterh is
> phosphorylated).
>
> Thanks!
>
>
>
> Ken Williams, Ph.D.
> Director, HHMI Biopolymer/Keck Laboratory
> Professor (Adjunct) Research
> Molecular Biophysics and Biochemistry
>
>
> Visit the HHMI Biopolymer/Keck Laboratory Web Page at:
>
> http://info.med.yale.edu/wmkeck/
>
>