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- W2169557911 abstract "Ovine casein macropeptide (CMP) was characterized by anion-exchange FPLC and reversed-phase (RP) HPLC. To study heterogeneity (the degree of glycosylation and phosphorylation), CMP was desialylated with neuraminidase and dephosphorylated with acid phosphatase. Following RP-HPLC, the main CMP components were identified using either on-line or off-line mass spectrometry. The most abundant ovine CMP component was a diphosphorylated carbohydrate-free form, followed by one or two monophosphorylated and a non-phosphorylated asialo-aglyco species. Aglyco non-phosphorylated, monophosphorylated and diphosphorylated forms were in the ratio 3[ratio ]20[ratio ]77. Only ∼ 30% of ovine CMP was glycosylated. Assuming that the monosaccharide fraction of ovine CMP is composed of N -acetylgalactosamine, galactose and N -glycolylneuraminic acid, molecular masses consistent with the presence of CMP containing tetra-, tri-, di- and monosaccharide were identified." @default.
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- W2169557911 date "2000-08-01" @default.
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- W2169557911 title "Chromatographic characterization of ovine κ-casein macropeptide" @default.
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- W2169557911 doi "https://doi.org/10.1017/s0022029900004222" @default.
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