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- W2000681883 abstract "Two sialyltransferases (EC 2.4.99.-) are extracted with Triton X-100 from human platelets and characterized with asialo 3H-labelled alpha 1-acid glycoprotein, an N-glycosylprotein. Methylation analysis of their specificities indicates that the enzymes transfer selectively sialic acid in a 3 or 6 position to oligosaccharides possessing Gal(beta 1-4)GlcNAc structure. The sialyl alpha 2-3 transferase was separated from the sialyl alpha 2-6 transferase by Ultrogel AcA34 column chromatography. Through affinity chromatography on CDPethanolamine-Sepharose, the two sialyltransferases are partly purified (5- and 20-fold enrichment of their specific activity, respectively, for sialyl alpha 2-3 transferase and alpha 2-6 transferase) and appear to be structurally heterogeneous." @default.
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- W2000681883 date "1984-07-01" @default.
- W2000681883 modified "2023-09-25" @default.
- W2000681883 title "Characterization of a sialyl α2–3 transferase and a sialyl α2–6 transferase from human platelets occurring in the sialylation of the N-glycosylproteins" @default.
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- W2000681883 doi "https://doi.org/10.1016/0167-4838(84)90266-8" @default.
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