Craig Webster wrote:
>> In article <jdb-230996164547 at wintermute.bioc.rice.edu>, John Bishop
> I use con A to bind glycoforms of alpha-1-acid glycoprotein (orosomucoid) in
> my work. As far as I know con A will bind to any protein that has bi-
> antennary glycans attached as this is the glycan motif that con A recognises.
Since many glycoscientists already answered the general question about Con A
binding, I'd like to commend on specific proteins that binds to Con A (I mean
binding, not just retarded).
Most lysosomal (or vacuole in yeast) proteins carry high mannose or hybrid
typed oligosaccharides, therefore, Con A was used primarily for the purifica-
tion of these enzymes or proteins in the early 70's. Specific enzymes include
beta-hexosaminidase, alpha-iduronidase (I am working on), alpha-glucosidase,
In addition, all N-linked glycoproteins were made in their early stages, as
glycoproteins carrying oligomannose structure, which were trimmed in the
ER to smaller structures, and re-glycosylated into complex structures.
Therefore, if an inhibitor of say, a mannosidase (e.g., swansonine) was
present, all of the N-linked glycoproteins could be bound to Con A.
Ke-Wei Zhao, Ph.D.
Dept. of Biol. Chem.
UCLA School of Medicine
Los Angeles, CA 90095-1737