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Two N-terminally truncated variants of human β-galactoside α2,6 sialyltransferase I with distinct properties for in vitro protein glycosylation.

Glycobiology - 1 Oct 2016

Luley-Goedl Christiane, Schmoelzer Katharina, Thomann Marco, Malik Sebastian, Greif Michael, Ribitsch Doris, Jung Christine, Sobek Harald, Engel Alfred, Mueller Rainer, Schwab Helmut, Nidetzky Bernd

Abstract excerpt

Sialic acid groups of protein N-glycans are important determinants of biological activity. Exposed at the end of the glycan chain, they are potential targets for glycan remodeling. Sialyltransferases (STs; EC 2.4.99) are the enzymes that catalyze the sialic acid transfer from a CMP-activated donor on to a carbohydrate acceptor in vivo. Recombinant expression of the full-length human β-galactoside α2,6...

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PMID: 27102286
DOI: 10.1093/glycob/cww046

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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