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Structural and functional characteristics of bovine milk protein glycosylation
Author(s) -
Noelle O’Riordan,
Marian Kane,
Lokesh Joshi,
Rita M. Hickey
Publication year - 2014
Publication title -
glycobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.757
H-Index - 128
eISSN - 1460-2423
pISSN - 0959-6658
DOI - 10.1093/glycob/cwt162
Subject(s) - glycoprotein , lactoferrin , glycosylation , bovine milk , glycan , oligosaccharide , chemistry , biochemistry , glycopeptide , casein , antibody , biology , immunology , antibiotics
Most secreted and cell membrane proteins in mammals are glycosylated. Many of these glycoproteins are also prevalent in milk and play key roles in the biomodulatory properties of milk and ultimately in determining milk's nutritional quality. Although a significant amount of information exists on the types and roles of free oligosaccharides in milk, very little is known about the glycans associated with milk glycoproteins, in particular, the biological properties that are linked to their presence. The main glycoproteins found in bovine milk are lactoferrin, the immunoglobulins, glycomacropeptide, a glycopeptide derived from κ-casein, and the glycoproteins of the milk fat globule membrane. Here, we review the glycoproteins present in bovine milk, the information currently available on their glycosylation and the biological significance of their oligosaccharide chains.

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