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Título

Heterogeneity of caprine κ-casein macropeptide

AutorMoreno, F. Javier ; Recio, Isidra ; Olano, Agustín ; López-Fandiño, Rosina
Palabras claveCaprine caseinmacropeptide
Phosphorylation
Genetic polymorphism
Mass spectrometry
Glycosylation
Fecha de publicación2001
EditorCambridge University Press
CitaciónJournal of Dairy Research 68(2): 197-208 (2001)
ResumenThe 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 monophosphorylated 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 diphosphorylated 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 diphosphorylated 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.
URIhttp://hdl.handle.net/10261/154970
DOI10.1017/S002202990100471X
Identificadoresdoi: 10.1017/S002202990100471X
issn: 0022-0299
e-issn: 1469-7629
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