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• W2151770837 endingPage "191" @default.
• W2151770837 startingPage "187" @default.
• W2151770837 abstract "SUMMARY k -Casein is the main glycoprotein of cow's milk. Its polysaccharide part is O -glycosidically linked to threonine residue 133. It contains only 3 different sugars (Gal, GalNAc, NeuNAc), but a microheterogeneity has been detected at the sugar level. Two main polysaccharides have so far been characterized. The structure of the trisaccharide is NeuNAc α → 3 Gal β1 →3 GalNAc; the tetrasaccharide contains one additional sialic acid. The polysaccharide part of ovine k -casein resembles that of bovine k -casein, but contains also N-glycolyl neuraminic acid. Human k -casein contains 3 times more carbohydrate than bovine k -casein with 2 additional sugars, GlcNAc and Fuc. The various polysaccharide parts isolated from bovine colostrum k -caseinoglycopeptide are much more complex than those obtained from the normal glycopeptide, indicating an evolution of the sugar part as a function of time after parturition. Some aspects of the secondary structure of k -casein and the role of the sugar part are discussed. The carbohydrate moiety of another milk protein, human lactotransferrin, is also discussed briefly. It is comprised of 2 identical glycan groups, N -glycosidically linked to the protein, and quite different from the k -casein carbohydrate moiety." @default.
• W2151770837 created "2016-06-24" @default.
• W2151770837 creator A5032028794 @default.
• W2151770837 date "1979-04-01" @default.
• W2151770837 modified "2023-10-18" @default.
• W2151770837 title "The carbohydrate portions of milk glycoproteins" @default.
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• W2151770837 doi "https://doi.org/10.1017/s0022029900017027" @default.
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