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Journal of Dairy Science Vol. 53 No. 9 1171-1176
© 1970 by American Dairy Science Association ®
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Effects of Varying Protein to Protein-Phosphate Ratios of {alpha}s-Casein on {alpha}s-K-Casein Micelles

David R. Whikehart1 and Gale W. Rafter

Department of Biochemistry, West Virginia University Medical Center, Morgantown 26506

ABSTRACT

Some properties of {alpha}s-{kappa}-casein micelles were studied with relation to the importance of protein-bound phosphate groups. Partial dephosphorylation of {alpha}s-casein by wheat germ acid phosphate decreased its incorporation into micelles. The micelles formed with dephosphorylated {alpha}s-casein were much smaller by electron microscopy than those formed with untreated {alpha}s-casein. Protein phosphate groups of {alpha}s-casein previously combined in a micelle were hydrolyzed by the acid phosphatase. Hydrolysis of the protein phosphate groups ultimately disrupted the micelle, which was pH dependent. {alpha}s-K-Casein micelles had porous or open structures through which macromolecules, such as acid phosphatase, gained access.

FOOTNOTES

1 Present address: Research Laboratory, McLean Hospital, Belmont, Massachusetts 02189.






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Copyright © 1970 by the American Dairy Science Association ®.