On 4 May 1995 11:42:25 -0700 Illimar Altosaar wrote:
> From: Illimar Altosaar <ALTOSAAR at ACADVM1.UOTTAWA.CA>
> Date: 4 May 1995 11:42:25 -0700
> Subject: (none)
> To: "bionet.glycosci mail newsgroup" <bionet-news at dl.ac.uk>
>> BSA is not glycosylated? David Ashford, you cite that with utmost confidence!
> Could I ask for references on that please? Especially the comment that most
> BSA preps contain glycosylated contaminants. All such studies will be most app
> reciated.
>> Illimar Altosaar, Biochemistry, University of Ottawa, Canada.
>I don't think the newsgroup should substitute for background reading or going to the library.
In answer to your specicfic questions:
BSA was originally sequenced as a protein and shown to contain no consensus sequence for N-glycosylation. No
O-glycosylation was found either. I don't have references for these results but I quess they would be published in
the 70s. BSA can be glycated (i.e. non-enzymic conjugation of the protein with free monosaccharides) in vitro. I
am not aware of measurements of the levels of glycated BSA in normal bovine blood. (Mainly because I haven't
looked; its not a great interest of mine).
BSA as generally described and unless otherwise specified contains contaminating bovine serum proteins; check
your Sigma catalogue. BSA is produced primarily by precipitation from serum by cold alcohol. Cohn fraction V is
99% pure at best. The remainder is mostly globulins, including gamma-globulins. One of the most common
proteins in serum after albumin is IgG, a glycoprotein. IgG is the predominant component of gamma-globulins.
David Ashford
Plant Glycoprotein Research Facility
Dept of Biology Univ of York
