The nature of the αs-casein complex of bovine milk has been investigated by cation-exchange chromatography on columns of sulphoethyl Sephadex C-50 of purified preparations of αs-casein and of whole acid-precipitated casein. Three main fractions were separated from each. Two behaved as single homogeneous proteins as judged by starch-gel electrophoresis; they were the main constituent of the complex, αs1-casein, and a closely related phosphoprotein, designated αs0-casein, which was present in small amounts only. The third fraction also constituted only a small part of the total complex. It was heterogeneous on starch gel electrophoresis and contained 2 major and 2 minor components. This fraction, while similar to other members of the αs-casein complex and to β-caseins hitherto described in that it contained phosphorus, nevertheless differed significantly from these since 3 at least of its components contained sulphur either in the form of disulphide bonds or of sulphydryl groupings.
Information is presented on the composition of the 3 fractions including C-terminal end group analysis.