Journal
BIOCHEMISTRY
Volume 48, Issue 41, Pages 9705-9707Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi901430h
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Funding
- NCRR NIH HHS [P41 RR005351, P41 RR005351-20, P41RR005351] Funding Source: Medline
- NIGMS NIH HHS [R37 GM033225, P41 GM103390, R01GM033225, R37 GM033225-24, R01 GM033225] Funding Source: Medline
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Sialylated forms of the Fc fragment of immunoglobulin G, produced by the human alpha 2-6 sialyltransferase ST6Gal-I, were identified as potent anti-inflammatory mediators in a mouse model of rheumatoid arthritis and are potentially the active components in intravenous IgG anti-inflammatory therapies. The activities and specificities of hST6Gal-I are, however, poorly characterized. Here MS and NMR methodology demonstrates glycan modification occurs in a branch-specific manner with the alpha 1-3Man branch of the complex, biantennary Fc glycan preferentially sialylated. Interestingly, this substrate preference is preserved when using a released glycan, suggesting that the apparent occlusion of glycan termini in Fc crystal structures does not dominate specificity.
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