Hi,
I'd like to weigh in with a related question and an answer would be much
appreciated: Would you expect a heated glycoprotein (say to 37C for 12 hr,
atmospheric pressure and RH) to make it reactive with a hydrazide-functional
agarose gel like CarboLink? One implication might be that the heating has
oxidized hydroxyls on the glycoprotein to aldehyde carbonyls, but is there
not a more likely explanation than that? Thanks,
Dan G
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Today's Topics:
1. Deglycosylation of N Oligosaccharides (Richard, Craig.)
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Message: 1
Date: Tue, 31 Jul 2007 13:56:15 -0400
From: "Richard, Craig." <crichard from su.edu>
Subject: [Protein-analysis] Deglycosylation of N Oligosaccharides
To: <proteins from magpie.bio.indiana.edu>, <doctorhim from aol.com>
Message-ID: <7EAAF58C8814494FB5A265C4F56C6611082DEC89 from suex2.su.edu>
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Harvey,
Checking to see if you are available for some endoglycosidase questions.
I've removed different Asn-linked carbohydrate chains from an intact
glycoprotein (non denatured, non reduced, non heated), but when I run it
on a non-reducing gel, some degly forms are the same MW as the non-degly
control, or are a larger MW than the degly control. Reducing gels give
clear confirmation of deglycosylation.
Share any thoughts if you like.
Thanks, Craig
Craig A. H. Richard Ph.D.
Assistant Professor, Biopharmaceutical Sciences
Bernard J. Dunn School of Pharmacy, Shenandoah University
1775 North Sector Court, Winchester, VA 22601
Phone: 540-678-4387 Fax: 540-665-1283
Email: crichard from su.edu <mailto:crichard from su.edu>
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