Glycosylation of κ-casein: I. Localization and characterization of sialyltransferase in bovine mammary gland
作者： S.J. Keller , T.W. Keenan , W.N. Eigel
DOI: 10.1016/0005-2744(79)90030-5
关键词:
摘要: Abstract A sialyltransferase ( CMP -N- acetylneuraminate: d -galactosyl-glycoprotein N- acetylneuraminyltransferase , EC 2.4.99.1) which attaches N -acetylneuraminic acid to the terminal end of carbohydrate chain κ-casein was found be concentrated in Golgi apparatus-enriched fractions bovine mammary gland. Maximum activity obtained at pH 5.5 and 37° presence 1 mM dithiothreitol Triton X-100. K m 0.19 mg asialo-κ-casein/ml (0.01 mM) for sialyltransferase. Native also served as acceptor transferase although a slower rate than did asialo-κ-casein. The has divalent cation requirement maximum best satisfied by 10 Mn 2+ .
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