01743naa a2200289 a 450000100080000000500110000800800410001910000220006024500960008226000090017852009690018765000210115665000110117765000110118865000180119965000220121765000130123965000100125265300080126265300170127065300180128765300300130570000140133570000140134970000240136377300660138720905632024-01-29       2000    bl uuuu     u00u1 u    #d1 aJAVIER MORENO, F.  aChromatographic characterization of ovine kappa-casein macropeptide.h[electronic resource]  c2000  aAbstract: 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.  aAcid phosphatase  aCasein  aCattle  aGlycosylation  aMass spectrometry  aPeptides  aSheep  aCMP  aMilk protein  aNeuraminidase  aOvine casein macropeptide1 aRECIO, I.1 aOLANO, A.1 aLÓPEZ-FANDIÑO, R.  tJournal of Dairy Researchgv. 6, n. 3, p. 349-359, Aug. 2000.