Abstract
Using 500-MHz 1H NMR spectroscopy we have investigated the branch specificity that bovine colostrum CMP-NeuAc:Galβ1→4GlcNAc-Rα2→6-sialyltransferase shows in its sialylation of bi-, tri-, and tetraantennary glycopeptides and oligosaccharides of the N- acetyllactosamine type. The enzyme appears to highly prefer the galactose residue at the Galβ1→4GlcNAcβ1→2Manα1→3 branch for attachment of the 1st
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