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The carbohydrate portions of milk glycoproteins

Published online by Cambridge University Press:  01 June 2009

Pierre Jollès
Pierre Jollès
Affiliation:
Laboratory of Proteins, University of Paris V, 45 rue des Saints-Pères, F-75270 Paris Cedex 06, France
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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.

Type
Section A. Biological Aspects of Milk Proteins
Information
Journal of Dairy Research , Volume 46 , Issue 2: Symposium on the Physics and Chemistry of Milk Proteins , April 1979 , pp. 187 - 191
Copyright
Copyright © Proprietors of Journal of Dairy Research 1979

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