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Journal of Dairy Science Vol. 56 No. 12 1559-1562
© 1973 by American Dairy Science Association ®
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Calcium Sensitivity and Molecular Weight of {alpha}s5-Casein1

S. J. Toma and S. Nakai

Department of Food Science, University of British Columbia, Vancouver 8, Canada

ABSTRACT

Alphas5-casein was more sensitive to calcium than {alpha}s1-casein, requiring 2 mM calcium chloride for 80% protein precipitation as compared to 8 mM for {alpha}s1-casein. Ability of {alpha}s5-casein to interact with K-casein forming micelles resistant to precipitation with calcium was less than that of {alpha}s1-casein.

Molecular weights determined by the differential boundary method in an ultracentrifuge were 65,750 and 31,800 for {alpha}s5-casein and for reduced {alpha}s5-casein (the equimolar mixture of {alpha}s3- and {alpha}s4-caseins). Elution of {alpha}s5-casein at the second half of the K-casein rich peak on Sephadex G-100 at pH 10.8 was ascribed to the molecular size of {alpha}s5-casein.

FOOTNOTES

1 Supported by Operating Grant A-3641 from the National Research Council of Canada.






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Copyright © 1973 by the American Dairy Science Association ®.