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Rapid separation of bovine caseins by mass ion exchange chromatography

Published online by Cambridge University Press:  01 June 2009

K. F. Ng-Kwai-Hang  and
J. P. Pélissier
K. F. Ng-Kwai-Hang
Affiliation:
Department of Animal Science, McGill University, 21, 111 Lakeshore Road, Ste Anne de Bellevue, P.Q., CanadaH9X 1CO
J. P. Pélissier
Affiliation:
Station de Recherches Laitières, Institut National de la Recherche Agronomique, CNRZ, 78350 Jouy-en-Josas, France
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Summary

The rapid isolation of major bovine caseins in gram quantities was investigated. Whole casein was precipitated from individual cow's milk by adjusting the pH to 4·6 and the precipitated casein was suspended in 4·5 M urea (pH 8·0) containing 0·02 M imidazole and 0·03 M β-mercaptoethanol, and bound on a QAE Zeta Prep 250 cartridge. Stepwise elution with the urea/imidazole β-mercaptoethanol buffer and varying amounts of NaCl gave five well resolved peaks, which were identified by polyacrylamide gel electrophoresis and fast protein liquid chromatography to be pure γ-casein, κ-casein. β-casein, β-casein and αs-casein, respectively. The ion exchange cartridge was regenerated by flushing with buffer containing 0·50 Μ-NaCl followed by equilibration with starting buffer before separation of next sample. The time required to run each sample including cartridge regeneration and equilibration was 4 hours.

Type
Original Articles
Information
Journal of Dairy Research , Volume 56 , Issue 3: Special Issue: Proceedings of the Hannah Research Institute Casein Conference , May 1989 , pp. 391 - 397
Copyright
Copyright © Proprietors of Journal of Dairy Research 1989

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