Glycosylated BSA?

David Ashford da5 at unix.york.ac.uk
Fri May 5 04:36:39 EST 1995

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  

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