Abstract
Abstract An improved method for the isolation of pure α S1 -casein from pooled milk is described. The method involves chemical isolation followed by DEAE-cellulose column-chromatographic fractionation. Alpha S1 -casein was characterized by SGUE, PGUE, chemical, and sedimentation analyses. The chromatographically pure α S1 -casein was found to contain α S1 -B and α S1 -C casein variants. These variants cannot be separated by DEAE-cellulose column chromatography. The preparation contained 1.10%P, equivalent to 10 phosphorus atoms per mole of 28,500. The molecular weight by approach to sedimentation equilibrium was 25,500. Alpha S1-casein in 0.1 M KCl, pH 5.6, showed random aggregation of 14S, while in tris-citrate buffer, pH 8.6, it showed 1.5 S, and in Na-PO4 buffer, pH 7.0, 4.2 S species.
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