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The binding of β-casein to hydroxyapatite: the effect of phosphate content and location

Published online by Cambridge University Press:  01 June 2009

Robert W. Sleigh ,
Thomas B. Sculley  and
Antony G. Mackinlay
Robert W. Sleigh
Affiliation:
School of Biochemistry, University of New South Wales, Kensington, New South Wales, Australia
Thomas B. Sculley
Affiliation:
School of Biochemistry, University of New South Wales, Kensington, New South Wales, Australia
Antony G. Mackinlay
Affiliation:
School of Biochemistry, University of New South Wales, Kensington, New South Wales, Australia
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Summary

The elution behaviour of β-casein from columns of hydroxyapatite has been studied and the effect examined of the enzymic addition of an extra phosphate residue. When the additional phosphate is located near pre-existing phosphate residues stronger binding to hydroxyapatite is observed. When the additional phosphate is remote from the pre-existing phosphates no increase in strength of binding is observed. It is suggested that the clustering of phosphate residues which characterizes αs- and β-caseins can be rationalized on the basis that it facilitates cooperative interactions between these phosphates and the Ca phosphate of the casein micelle and/or basic residues within casein polypeptide chains.

Type
Section D. Casein Micelles
Information
Journal of Dairy Research , Volume 46 , Issue 2: Symposium on the Physics and Chemistry of Milk Proteins , April 1979 , pp. 337 - 342
Copyright
Copyright © Proprietors of Journal of Dairy Research 1979

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References

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