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Abstract
Beta-casein from individual buffalo's milk was found to be homogeneous by starch-gel electrophoresis. Beta-Casein was separated from buffalo's milk by the method of Warner (1944) and purified by DEAE-cellulose chromatography. Buffalo beta-casein possesses identical end-groups to those of cow beta-casein; namely N-terminal arginine and assuming a single polypeptide chain a possible C-terminal sequence of Ile-Ile-Val. However, the amino-acid composition and the trypic peptide patterns of the 2 proteins are not the same.
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