Studies on the Heterogeneity of Crystallized β-Lactoglobulin in Cow's Milk

Abstract

Crystalline β-lactoglobulin was prepared from Japanese COW'S milk by the improved method of R. ASCHAFFENBURG. Its heterogeneity was demonstrated by its partial resolution into the two components by the paper and Tiselius electrophoresis.
Crystalline β-lactoglobulin was fractionated by a chromatography on DEAE cellulose column to yield the different proteins β-lactoglobulin A and B in high purity.
The differences in the optical rotatory power, (N)_??_(R) transition and polypeptides from reductive cleavage of disulfide bound of β-lactoglobulin between forms A and B were examined. The results suggest that there may be only slight differences between forms A and B.