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Heterogeneity of caprine κ-casein macropeptide

  • F. JAVIER MORENO (a1), ISIDRA RECIO (a1), AGUSTÍN OLANO (a1) and ROSINA LÓPEZ-FANDIÑO (a1)

Abstract

The heterogeneity of caprine caseinmacropeptide (CMP) was determined by means of treatments with neuraminidase and acid phosphatase and analyses by anion exchange FPLC and reversed-phase (RP)-HPLC, with on-line and off-line electrospray ionization mass spectrometry. The main CMP components were two non-glycosylated and di-phosphorylated forms, as well as two other mono-phosphorylated species, each corresponding to a genetic variant of caprine κ-casein due to the silent substitution Ile/ Val at position 119. Asialo-aglyco mono- and di-phosphorylated forms were found in the ratios 8–14% and 86–92%, respectively. Approximately 36% of caprine CMP was glycosylated. Based on the obtained molecular masses, the occurrence of tri-, di- and monosaccharide-containing di-phosphorylated CMP are reported, assuming that N-acetylgalactosamine, galactose, N-acetyl and N-glycolylneuraminic acids would constitute the main monosaccharides of caprine CMP. CMP microheterogeneity due to the genetic polymorphism was also observed in the glycosylated forms.

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For correspondence: rosina@ifi.csic.es

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