Chromatographic characterization of ovine kappa-casein macropeptide.


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 3:20:77. Only approximately 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.

Cite this paper

@article{Moreno2000ChromatographicCO, title={Chromatographic characterization of ovine kappa-casein macropeptide.}, author={Francisco A. Moreno and Isidra Recio and Agust{\'i}n Olano and R L{\'o}pez-Fandi{\~n}o}, journal={The Journal of dairy research}, year={2000}, volume={67 3}, pages={349-59} }