Action of Rennin on κ-Casein, the Amino Acid Compositions of the Para-κ-Casein, and Glycomacropeptide Fractions

Abstract

The action of rennin on K-casein obtained from the milk of an individual cow was investigated. Polyacrylamide-gel electrophoresis at pH 9.2 indicated the presence of two major components in reduced pard-K-casein. The amino acid compositions of K-casein, para-K-easein, and the glycomacropeptide were compared.