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Registro Completo |
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Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
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Data corrente: |
21/05/2024 |
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Data da última atualização: |
21/05/2024 |
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Autoria: |
JOLLÈS, P.; FIAT, A. M. |
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Título: |
The carbohydrate portions of milk glycoproteins. |
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Ano de publicação: |
1979 |
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Fonte/Imprenta: |
Journal of Dairy Research, v. 46, n. 2, p. 187-191, Apr. 1979. |
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DOI: |
https://doi.org/10.1017/S0022029900017027 |
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Idioma: |
Inglês |
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Conteúdo: |
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. |
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Palavras-Chave: |
Amino acid sequence; Species specificity. |
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Thesaurus Nal: |
Carbohydrates; Cattle; Cows; Glycoproteins; Milk analysis; Milk proteins; Molecular conformation; Oligosaccharides; Sheep; Sialic acids. |
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Categoria do assunto: |
L Ciência Animal e Produtos de Origem Animal |
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Marc: |
LEADER 02061naa a2200289 a 4500
001 2164363
005 2024-05-21
008 1979 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1017/S0022029900017027$2DOI
100 1 $aJOLLÈS, P.
245 $aThe carbohydrate portions of milk glycoproteins.$h[electronic resource]
260 $c1979
520 $ak-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.
650 $aCarbohydrates
650 $aCattle
650 $aCows
650 $aGlycoproteins
650 $aMilk analysis
650 $aMilk proteins
650 $aMolecular conformation
650 $aOligosaccharides
650 $aSheep
650 $aSialic acids
653 $aAmino acid sequence
653 $aSpecies specificity
700 1 $aFIAT, A. M.
773 $tJournal of Dairy Research$gv. 46, n. 2, p. 187-191, Apr. 1979.
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Registro original: |
Embrapa Caprinos e Ovinos (CNPC) |
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