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Human Casein. III. DEAE-Celluslose-Urea Chromatography of Human Casein and Dephosphorylation of Casein Fractions

Central Research Laboratory, Morinaga Milk Industry Company, Ltd., Tokyo, Japan

ABSTRACT

Human casein was separated into at least 11 fractions by DEAE cellulose column chromatography in 3.3 M urea. Addition of 2-mercaptoethanol did not improve sharpness of peaks, nor homogeneity of fractions. Electrophoretic mobility of the main six fractions increased with phosphorus content.

Human ß-casein A through E was readily dephosphorylated by phosphoprotein phosphatase from beef spleen. Partial dephosphorylation of human ß-casein A and bovine ß-casein was accompanied by the appearence of five new components with lower nlobilities and gel electrophoretic patterns of these components resembled those of human casein's main six cornponents. Dephosphorylated human ß-casein A through E had the slowest-moving band corresponding to phosphorus-free ß-casein F on gel electrophoresis. Human ß-casein A, the most highly phosphorylated fraction resembled bovine ß-casein in phosphorus content, calcium sensitivity, and electrophoretic mobility. Human ß-caseins, main six components of human casein, are composed of a single protein with 0 to 5 atonis of phosphorus per molecule.