Abstract
Purified K-casein was hydrolyzed with Pronase P and the resultant hydrolysate was fractionated by column chromatography. A glycopeptide was isolated which contained approximately 64% total carbohydrate (hexose, hexosamine, sialic acid) and no detectable amount of phosphorus. Calculations based on the amino acid composition of the glycopeptide gave a minimal molecular weight of 11,000. The glycopeptide had no N-terminal amino acid and carboxypeptidase liberated only serine. On the basis of a molecular weight of 11,000, the peptide contained 39amino acid residues(ll threonine, 7 serine) and 6, 14 and 16 residues of sialic acid, hexose and hexosamine, respectively.

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