Presence of o-glycosidic linkage through serine residue in k-casein component from bovine mature milk.
- 1 January 1981
- journal article
- research article
- Published by Center for Academic Publications Japan in Journal of Nutritional Science and Vitaminology
- Vol. 27 (3) , 231-241
- https://doi.org/10.3177/jnsv.27.231
Abstract
This paper describes the glycosylation sites of .kappa.-casein component P-5 from bovine mature milk. A short glycopeptide was prepared from .kappa.-casein component P-5 containing 2 carbohydrate chains by pronase P digestion, followed by gel filtration and ion exchange chromatographies. The glycopeptide obtained corresponded to residues 128-141 (Gly-Glu-Pro-Thr-Ser-Thr-Pro-Thr-Thr-Glu-Ala-Val-Glu-Ser) of .kappa.-casein A from the results of analyses with chemical and enzymatic procedures. The effect of alkaline borohydride treatment indicated the presence of serine and threonine as the binding site of carbohydrate moieties. From the facts of Edman degradation and carboxypeptidase P hydrolysis of glycopeptide treated with alkali, the carbohydrate moieties were considered to be attached to threonine residue No. 133 and serine residue No. 141.This publication has 3 references indexed in Scilit:
- Attachment Sites of Carbohydrate Moieties to Peptide Chain of Bovineκ-Casein from Normal MilkAgricultural and Biological Chemistry, 1980
- β-turns in proteinsJournal of Molecular Biology, 1977
- Chromatographic Isolation and Partial Characterization of Reduced κ-Casein Components*Biochemistry, 1966