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Journal of Dairy Science Vol. 55 No. 8 1041-1049
© 1972 by American Dairy Science Association ®
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Composition of Bovine {gamma}-Caseins A1 and A3, and Further Evidence For a Relationship in Biosynthesis of {gamma}- and ß-Caseins

M. L. Groves, W. G. Gordon, E. B. Kalan and S. B. Jones

Eastern Marketing and Nutrition Research Division, USDA, Philadelphia, Pennsylvania 19118

ABSTRACT

Two variants, A1 and A3, of {gamma}- and ß-caseins were isolated from samples of bovine milk which were typed as homozygous for ß-casein A1 or A3. {gamma}- and ß-Caseins A1 and A3 differ in amino acid composition by two residues of histidine and the data suggest that the same substitutions, His/Gln and His/Gln or His/Pro distinguish the {gamma}- and ß-variant pairs. {gamma}- ß-casein polyrnorphs Al, A2, A3 and B all have a common C-terminal sequence -Ile-Ile-Val OH and they show similar chymotryptic peptide maps. They differ in their N-terminal amino acids: arginine for ß-caseins and lysine for {gamma}-caseins. {gamma}-Casein is smaller than ß-casein by about 28 amino acid residues. It is possible that {gamma}-casein is identical with a large portion of ß-casein.






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Copyright © 1972 by the American Dairy Science Association ®.