Formation of lysinoalanine from individual bovine caseins
- 1 June 1980
- journal article
- research article
- Published by Cambridge University Press (CUP) in Journal of Dairy Research
- Vol. 47 (2) , 193-198
- https://doi.org/10.1017/s0022029900021063
Abstract
Summary: The formation of lysinoalanine, N-є-(2-amino-2-carboxyethyl)-L-lysine, by treatment of αs0-, αsl- and β-casein with alkali, has been studied. In all 3 proteins lysinoalanine was formed by reaction of lysyl residues with dehydroalanyl residues produced by alkaline degradation of those phosphoseryl residues which occupy isolated positions in the proteins' structures. The contribution to lysinoalanine production made by phosphoseryl residues which were arranged in clusters, as occurs in the sequence -Ser(P)-Ser(P)-Ser(P)-, was not significant.This publication has 14 references indexed in Scilit:
- Covalent bonds formed in proteins during milk sterilization: studies on caseins and casein peptidesJournal of Dairy Research, 1979
- The reaction of αs1- and β-casein with ferrous ions in the presence of oxygenJournal of Dairy Research, 1978
- Bovine alphaso Casein; a Phosphorylated Homologue of alphas1 CaseinEuropean Journal of Biochemistry, 1977
- αs0-Casein: its preparation and characterizationJournal of Dairy Research, 1976
- Lysinoalanine: Presence in Foods and Food IngredientsScience, 1975
- The alkali-induced elimination of phosphate from β-caseinJournal of Dairy Research, 1972
- The structure of a phosphopeptide derived from β-caseinArchives of Biochemistry and Biophysics, 1971
- Nδ-(2d-amino-2-carboxyethyl)-ornithine, a New Amino-acid from Alkali-treated ProteinsNature, 1967
- Automatic Recording Apparatus for Use in Chromatography of Amino AcidsAnalytical Chemistry, 1958
- The estimation of phosphorusBiochemical Journal, 1940