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Isolation and characterization of the principal caseins in rat milk

Published online by Cambridge University Press:  01 June 2009

Jean-Pierre Pelissier
Affiliation:
Laboratoire de Biochimie et de Technologie Laitières, CNRZ, IN RA 78350 – Jouy-en-Josas, France
Ahmed Yahia
Affiliation:
Laboratoire ISTA, CNAM, 292 rue St-Martin, 75003 – Paris, France
Jean-Marc Chobert
Affiliation:
Laboratoire de Biochimie et de Technologie Laitières, CNRZ, IN RA 78350 – Jouy-en-Josas, France
Bruno Ribadeau Dumas
Affiliation:
Laboratoire de Biochimie et de Technologie Laitières, CNRZ, IN RA 78350 – Jouy-en-Josas, France

Summary

The 4 major caseins, A1, A2, B1, B2, from rat milk have been isolated and analysed. From molecular weight determination, amino acid and phosphorus analyses and N-terminal sequence determination, A1 and A2 are concluded to possess similar peptide chains as do B1 and B2, with the individual fractions within each of these 2 groups differing only in their sialic acid content.

Mol. wts of approximately 22000 and 38000 were found for A1–A2 and B1–B2 respectively. The amino acid sequence of the first 13 residues of A1–A2 has been partly established. Components A1 and A2 appeared to be homologous with bovine β-casein, whereas B1 and B2 were different from any known casein, especially in their molecular weight.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1980

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