Author:
Baumy J.-J.,Guenot P.,Sinbandhit S.,Brulé G.
Abstract
SummaryThe effect of Ca2+. binding and ionic strength on the physicochemical characteristics of phosphoserine residues was studied on O-phospho-DL-serine, bovine β-casein and its phosphopeptide (1–25) using 31P NMR. pK in various experimental conditions were determined.The pK of the phosphoserine residues of β-casein and its phosphopeptide (1–25) respectively ranged from 6·46 to 7·21 and from 6·57 to 7·10. pK of O-phospho-DL-serine, β-casein and its phosphopeptide decreased when Ca2+ was bound to the phosphoserine residue or when ionic strength was increased. The binding of Ca2+ to the phosphopeptide (1–25) took place at first on phosphoserine residues 17, 18, 19 which had the highest pK, then, when these were saturated, on residue 15 whose pK was the lowest. When the four sites had bound Ca2+, peaks corresponding to a different complex form appeared in the spectrum.
Publisher
Cambridge University Press (CUP)
Subject
Animal Science and Zoology,General Medicine,Food Science
Reference16 articles.
1. Baumy J. J. & Brulé G. 1988 Effect of pH and ionic strength on the binding of bivalent cations to β-casein. Lait (In the Press)
2. Brulé G. , Roger L. , Fauquant J. & Piot M. 1980 Procédé de traitement d'une matière première à base de caséine contenant des phosphocaséinates de cations monovalents et leurs dérivés. French patent no. 80 02 281
3. Nuclear magnetic resonance titration curves of histidine ring protons. II
4. A Preliminary study of the calcium binding to β-casein using 31P Nuclear Magnetic Resonance (NMR);Humphrey;XXIst International Dairy Congress Moscow,1982
5. The 31P nuclear magnetic resonance spectrum of cows' milk
Cited by
52 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献