Elektrophoretische Differenzierung von Säure- und Labcasein

Summary

The electrophoretic patterns of normal casein (precipitated with acid from cow's milk) and of rennetcasein obtained in a veronal buffer at ap _H of 7.3 are remarkably different from each other. The ascending boundary of the α-fraction of casein treated with rennet splits off into two peaks showing the presence of two subfractions (α₁ and α₂). The proportion of quantity of the faster (α₁) and of the slower (α₂) subfraction was found to be about 0.9:1. The α-component of casein which was not treated with active rennet behaved under the same conditions electrophoretically uniform.