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J Chromatogr A. 1995 Aug 4;708(2):223-30.

Heterogeneity of the bovine kappa-casein caseinomacropeptide, resolved by liquid chromatography on-line with electrospray ionization mass spectrometry.

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Institut National de la Recherche Agronomique, Laboratoire de Recherches de Technologie Laitière, Rennes, France.


Microheterogeneity occurs in the population of caseinomacropeptides (residues 106-169 of kappa-casein) due to variation in the extent and type of oligosaccharide linked to this phosphoglycopeptide. Although caseinomacropeptide A variant (CMPA) was poorly resolved using reversed-phase high-performance liquid chromatography (RP-HPLC) with spectrophotometric detection, it could be analysed with on-line electrospray-ionization mass spectrometry (ESI-MS). From the already established O-linked glycan chains at least fourteen glycosylated forms of CMPA were identified, besides the non-glycosylated and multiphosphorylated (1, 2 or 3 phosphate groups) peptides, giving a maximum number of eighteen known forms. Major subcomponents in CMPA are disialylated species. A maximum of three out of the five potential glycosylation sites were found to be substituted with carbohydrate chains in the most highly glycosylated forms, which may contain up to six N-acetylneuraminic acid residues per molecule. A minor form, diphosphorylated with one disialylated chain, was also detected. From these results, it was shown that the on-line coupling of HPLC with ESI-MS offers a very promising alternative for the analysis of complex mixtures.

[Indexed for MEDLINE]

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