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Identification of the -Casein Among the Components of Whole Goat Casein

Eastern Regional Research Laboratory, Eastern Utilization Research and Development Division, USDA, Philadelphia, Pennsylvania

ABSTRACT

Goat -casein in the reduced state, probably the natural state, has a mobility on acrylamide gel electrophoresis at pH 9, very close to that of the ß-caseins. The goat -casein was identified by clotting with rennin, by specific changes in the electrophoretic pattern after rennin action, and by nonprecipitation with calcium ions. It stabilized goat _s-casein so that as-casein was not precipitated with calcium ions. Polyacrylamide gel electrophoresis of goat -casein in some cases gave a single band (together with identifiable contaminants), and, in other cases, gave a multiplicity of slower-moving bands. In all cases only a single major band was observed when the -casein was reduced with mercaptoethanol. Components with the mobilities of para--casein were present in considerable amounts in some preparations of -casein.