ConA binding all N-glycosylated animal proteins?

Iain Wilson WILSON at edv1.boku.ac.at
Thu Apr 27 09:06:47 EST 1995

> Date:          Tue, 25 Apr 1995 21:11:22 GMT
> From:          christer.ericsson at mog.ki.se (Christer Ericsson)
> Reply-to:      christer.ericsson at mog.ki.se (Christer Ericsson)
> To:            "bionet.glycosci mail newsgroup" <bionet-news at dl.ac.uk>
> Subject:       ConA binding all N-glycosylated animal proteins?

> Is it fair to say that concanavalin A binds to most (or to all)
> N-glycosylated animal proteins through its capacity to bind to internal or
> terminal mannose or glucose residues. What specifically is missed? How
> large a fraction are these of the total?

ConA binding 'rules' may have to be made into a FAQ: a few weeks back 
I responded to a query on O-linked mannose binding to ConA! Here 
goes for a cut-and-paste:

 Going by the 'rules', Con A would not bind O-linked mannose. (See 
 Kobata and Yamashita in Glycobiology A Practical Approach, p. 110 - 
 they refer to a previous Kobata paper and state that ConA 'interacts 
 with sugar chains which have two non-substituted or C-2 substituted 
 alpha-mannopyranosyl residues in one molecule') 

Thus by the same rule tri-, tetra, and penta-antennary N-links will 
not bind ConA since they will have 1,4 and 1,6 linked GlcNAc 
residues.  As for the fraction not bound - it depends on your 
source. Are there any ConA experts out there to add more info?


Iain Wilson                        Institut fuer Chemie           
Tel: 43-1-47654-6065               Universitaet fuer Bodenkultur   
Fax: 43-1-310-5176                 Gregor-Mendel-Strasse 33
E-mail: wilson at edv1.boku.ac.at     A-1180, WIEN, Austria


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