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A 20,000-Dalton Casein Fragment in Human Milk¹

Department of Agricultural Chemistry, The University of Tokyo, Bunkyo-ku, Tokyo 113, Japan

ABSTRACT

A new peptide of 20,000 daltons was found in human milk as a constituent of the casein micelle. Enzymic digestion with plasmin or trypsin revealed that the peptide was identical with a degradation product of human ß-casein. The amino acid composition of the degradation product and the previously reported sequence in the N-terminal region of human ß-casein suggested that the peptide was a fragment of ß-casein lacking the C-terminal region. The thermal sensitivity of this peptide was higher than that of ß-casein, but the peptide lost the property of calcium-dependent precipitation, which intact ß-casein possesses.

¹ This work was supported by a grant for scientific research from the Ministry of Education, Science and Culture, Japan (57,470,096).