Bovine alphaso Casein; a Phosphorylated Homologue of alphas1 Casein
- 1 September 1977
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 78 (2) , 411-417
- https://doi.org/10.1111/j.1432-1033.1977.tb11753.x
Abstract
After consideration of its electrophoretic behavior, amino acid composition and phosphate content, bovine .alpha.s0 casein was shown to differ from .alpha.s1 casein only in respect of its phosphate content. The presence in .alpha.s0 casein of 1 phosphate residue more than occurs in .alpha.s1 casein was confirmed by comparative degradative studies performed on both proteins. From these it was concluded that .alpha.s0 casein may be considered as being .alpha.s1 casein which was modified by phosphorylation of the seryl residue located at position 41.This publication has 11 references indexed in Scilit:
- αs0-Casein: its preparation and characterizationJournal of Dairy Research, 1976
- Chromatographic separation of β-methyldiaminopropionic acid in hydrolysates of modified phosphoproteins in an amino acid analyzerJournal of Chromatography A, 1972
- The alkali-induced elimination of phosphate from β-caseinJournal of Dairy Research, 1972
- Structure primaire de la caséine αsl‐bovineEuropean Journal of Biochemistry, 1971
- The structure of a phosphopeptide derived from β-caseinArchives of Biochemistry and Biophysics, 1971
- A fractionation of the αs-casein complex of bovine milkJournal of Dairy Research, 1969
- Modified Procedure of Starch Gel Electrophoresis for β-Casein PhenotypingJournal of Dairy Science, 1966
- Automatic Recording Apparatus for Use in Chromatography of Amino AcidsAnalytical Chemistry, 1958
- The estimation of phosphorusBiochemical Journal, 1940