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Electrophoretic Studies of Commercial and Iodinated Casein¹

Department of Dairy Husbandry, University of Missouri, Columbia

ABSTRACT

An electrophoretic study of commercial casein, iodinated casein, and Prota-mone was made in a new model no. 38 electrophoresis apparatus (Perkin-Elmer Corp.).

It was observed that casein consists of an and ß component. The observations of other investigators of the electrophoretic pattern of casein were confirmed.

It was observed that Protamone, unlike its mother substance casein, was homogeneous electrophoretically.

The electrophoretic mobility of Protamone was –6.0 to –9.2^10–5 at pH 6.0, 8.3 and 7.5 in acetate and barbiturate buffers with an ionic strength of 0.1. Furthermore, the electrophoretic mobility of Protamone was significantly higher than either or ß-casein under all the conditions studied.

It also was observed that incubation with stirring of casein at 39° C. did not change the electrophoretic pattern in barbiturate buffer pH 7.5 with an ionic strength of 0.1. However, when iodine was added the electrophoretic pattern was changed and only a small peak of ß-casein was observed.

Casein incubated at 70° C. with or without iodination when studied electrophoretically in barbiturate buffer pH 7.5 with an ionic strength of 0.1 showed a single peak.

¹ Contribution from the Department of Dairy Husbandry, Missouri Agricultural Experiment Station, Journal Series no. 1171.