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Purification and characterization of porcine κ-casein

Published online by Cambridge University Press:  01 June 2009

Jutta Cerning-Beroard  and
Claude Zevaco
Jutta Cerning-Beroard
Affiliation:
Laboratoire de Biochimie et Technologie Laitières, Institut National de la Recherche Agronomique, CNRZ, 78350 Jouy-en-Josas, France
Claude Zevaco
Affiliation:
Laboratoire de Biochimie et Technologie Laitières, Institut National de la Recherche Agronomique, CNRZ, 78350 Jouy-en-Josas, France
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Summary

κ-casein from porcine milk was isolated and purified by affinity chromatography on thiopropyl Sepharose followed by hydroxyapatite chromatography. The amino acid composition of this protein is similar to that of bovine κ-casein. The sugar composition was established and sow κ-casein was found to be highly glycosylated. It contains 12 N-acetylneuraminic acid, 10 N-acetylgalactosamine, 2 N-acetylglucosamine and 22 galactose residues.

Type
Original Articles
Information
Journal of Dairy Research , Volume 51 , Issue 2 , May 1984 , pp. 259 - 266
Copyright
Copyright © Proprietors of Journal of Dairy Research 1984

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