From: Jim Bloom <Jim.Bloom.B@bayer.com>
  To  : -         *rasmb@alpha.bbri.org <rasmb@alpha.bbri.org>
  Date: Thu, 27 Apr 2000 16:29:51 -0400

Incompetence..

 Many thanks to Borries, Tom and Yujia Xu for their lucid explanations
of incompetence and competence.  I have had an interesting thought for the
biochemically inclined.  I do much more ESI-MS analysis than AUC and therefore
see lots of subtle differences in proteins.  We also work with glycosylated
proteins.  Examples are an interleukin that contained four forms:  a full
length non-glycosylated, des1-2 non-glycosylated (ie. biochemists
jargon....lacking the first two amino acids on the N-terminal), and two
glycosylated full length versions.  We also have another protein with a full
length non-glycosylated population and  glycosylated at one N-linked site and
glycosylated at two sites.   So, with this background comes a topic of interest
to me: are these forms of the same molecule structurally "the same".   In the
experience of the RASMBer's, has anyone seen a difference...for example maybe
one might see aggregation with the non-glycosylated forms but not the
glycosylated?
 One other comment...in a discussion with John Philo at one time he
mentioned to me that in a sense using AUC with glycosylated proteins is a
"waste of time" ie. too much heterogeneity.  Any comments on this issue?
 Jim