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Chromatographic characterization of ovine κ-casein macropeptide

AutorMoreno, F. Javier ; Recio, Isidra ; Olano, Agustín ; López-Fandiño, Rosina
Fecha de publicación2000
EditorCambridge University Press
CitaciónJournal of Dairy Research 67(3): 349-359 (2000)
ResumenOvine 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 asialoaglyco species. Aglyco non-phosphorylated, monophosphorylated and diphosphorylated forms were in the ratio 3:20:77. 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.
URIhttp://hdl.handle.net/10261/154967
DOI10.1017/S0022029900004222
Identificadoresdoi: 10.1017/S0022029900004222
issn: 0022-0299
e-issn: 1469-7629
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