Casein. VIII. Isolation of a Glycopeptide from an Enzymic Hydrolysate of κ-Casein
Open Access
- 1 August 1967
- journal article
- research article
- Published by American Dairy Science Association in Journal of Dairy Science
- Vol. 50 (8) , 1206-1210
- https://doi.org/10.3168/jds.s0022-0302(67)87600-8
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.This publication has 15 references indexed in Scilit:
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