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Human Neuraminidases Have Reduced Activity Towards Modified Sialic Acids on Glycoproteins

preprint
revised on 21.08.2020, 01:55 and posted on 21.08.2020, 07:47 by Carmanah D. Hunter, Elizabeth Porter, Christopher Cairo
This work investigated the substrate specificity of hNEU enzymes for a glycoprotein substrate (bovine submaxillary mucin) containing 9-O-acetylated and Neu5Gc residues. Using this model substrate, we observe a general trend for hNEU tolerance of Neu5Ac>Neu5Gc>>>Neu5,9Ac2, consistent with our previous results with glycolipid substrates. These results expand our understanding of hNEU enzyme specificity and suggest that naturally occurring modifications of sialic acids can play a role in regulating hNEU activity.

Funding

Natural Sciences and Engineering Research Council of Canada (NSERC)

Natural Sciences and Engineering Research Council

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History

Email Address of Submitting Author

ccairo@ualberta.ca

Institution

University of Alberta

Country

Canada

ORCID For Submitting Author

0000-0003-3363-8708

Declaration of Conflict of Interest

No conflicts of interest declared.

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