> 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
---------------------------------------------------------------
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
http://www-bprc.mps.ohio-state.edu/cgi-bin/hpp/iain_wilson.html
