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Study of calcium binding to phosphoserine residues of β-casein and its phosphopeptide (1–25) by 31P NMR

Published online by Cambridge University Press:  01 June 2009

J.-J. Baumy ,
P. Guenot ,
S. Sinbandhit  and
G. Brulé
J.-J. Baumy
Affiliation:
Laboratoire de Recherche de Technologie Laitière, Institut National de la Recherche Agronomique, 65, Rue de Saint Brieuc, 35042 Rennes Cedex, France
P. Guenot
Affiliation:
Laboratoire de Résonance Magnétique Nucléaire, Centre Régional de Mesures Physiques de L'Ouest, Campus de Beaulieu, 35042 Rennes Cedex, France
S. Sinbandhit
Affiliation:
Laboratoire de Résonance Magnétique Nucléaire, Centre Régional de Mesures Physiques de L'Ouest, Campus de Beaulieu, 35042 Rennes Cedex, France
G. Brulé
Affiliation:
Laboratoire de Recherche de Technologie Laitière, Institut National de la Recherche Agronomique, 65, Rue de Saint Brieuc, 35042 Rennes Cedex, France
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Summary

The 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.

Type
Original Articles
Information
Journal of Dairy Research , Volume 56 , Issue 3: Special Issue: Proceedings of the Hannah Research Institute Casein Conference , May 1989 , pp. 403 - 409
Copyright
Copyright © Proprietors of Journal of Dairy Research 1989

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References

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