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Casein. VIII. Isolation of a Glycopeptide from an Enzymic Hydrolysate of -Casein¹

Macdonald College of McGill University, Macdonald College, P.Q., Canada

ABSTRACT

-Casein was hydrolyzed with Pronase P and the resultant hydrolysate was fractionated on Sephadex G-50. 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 39 amino acid residues (11 threonine, 7 serine) and 6, 14, and 16 residues of sialic acid, hexose, and hexosamine, respectively.

¹ Macdonald College Journal Series no. 566.