Periodate doesn't remove carbohydrate - it oxidizes it to give other
functional groups which may be great for some purposes, but probably not
desirable as an immunogen. (Though if you used the oxidized protein to
screen hybridomas generated from the native protein at least you
wouldn't be selecting for the carbohydrate binding ones.) Check out
http://www.prozyme.com/glycopro/ge50kit.html
for info on how to deglycosylate the protein (enzymes are available from
other sources as well).
John Russell
Chris Weir wrote:
> Hi all,
> I hoping someone out there maybe able to give me some ideas. I
> am currently making antibodies to a protein which has high levels of
> glycosylation. I have made several mAbs now to the glycosylated
> section but want to make some to the non-glycosylated section. It
> appears that the glycosylated section is immunodominant. I was
> thinking of using sodium periodate to remove the glycosylation and
> hopefully expose the other antigens (and get mabs to them) but if
> anyone has any other ideas/suggestions it would be greatly
> appreciated.
>> Thanks in advance
> Chris Weir
> Australian Envirionmental Flow Cytometry Group
> School of Biological Sciences
> Macquarie University
> Sydney, NSW, 2109
> Australia
> ph 61 2 9850 8150
> fax 61 2 98508253
> email: cweir at rna.bio.mq.edu au
