Hostname: page-component-7bb8b95d7b-lvwk9 Total loading time: 0 Render date: 2024-10-01T14:32:18.515Z Has data issue: false hasContentIssue false
  • English
  • Français

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
Get access Rights & Permissions [Opens in a new window]

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

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Addeo, F., Chobert, J. -M. & Ribadeau-Dumas, B. (1977). Journal of Dairy Research 44, 63.CrossRefGoogle Scholar
Abnone, A. (1972). Nature, London 237, 146.Google Scholar
Bernardi, G. (1973). In Methods in Enzymology, vol. XXVII p. 471. (Eds Hirs, C. H. W. and Timasheff, S. N..) New York: Academic Press.Google Scholar
Burley, R. W. & Cook, W. H. (1962). Canadian Journal of Biochemistry and Physiology 40, 373.CrossRefGoogle Scholar
Evans, M. T. A., Irons, L. & Jones, M. (1971). Biochimica et Biophysica Acta 229, 411.CrossRefGoogle Scholar
Kemp, B. E., Bylund, D. B., Huang, T. -S. & Krebs, E. G. (1975). Proceedings of the National Academy of Sciences of the USA 72, 3448.CrossRefGoogle Scholar
Kleinsmith, L. J. & Allfrey, V. G. (1969). Biochimica et Biophysica Acta 175, 123.CrossRefGoogle Scholar
Leslie, R. B., Irons, L. & Chapman, D. (1969). Biochimica et Biophysica Acta 188, 237.CrossRefGoogle Scholar
Manson, W. & Annan, W. D. (1971). Archives of Biochemistry and Biophysics 145, 16.CrossRefGoogle Scholar
Manson, W., Carolan, T. & Annan, W. D. (1977). European Journal of Biochemistry 78, 411.CrossRefGoogle Scholar
Noelken, M. & Reibstein, M. (1968). Archives of Biochemistry and Biophysics 123, 397.CrossRefGoogle Scholar
Posner, A. S. & Betts, F. (1975). Accounts of Chemical Research 8, 273.CrossRefGoogle Scholar
Rose, D. & Colvin, J. R. (1966). Journal of Dairy Science 49, 351.CrossRefGoogle Scholar