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Binding of calcium ions to bovine β-casein

Published online by Cambridge University Press:  01 June 2009

Thomas G. Parker  and
Douglas G. Dalgleish
Thomas G. Parker
Affiliation:
The Hannah research Institute, Ayr, Scotland, KA6 5HL
Douglas G. Dalgleish
Affiliation:
The Hannah research Institute, Ayr, Scotland, KA6 5HL
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Summary

The isotherms for Ca2+ binding to bovine β-casein have been measured at 5 temperatures in the range 4–40 °C and at 4 different ionic strengths. The results are interpreted by an interactive-site binding model, and are compared with results previously obtained on αs1-casein. The affinity of β-cesein for the first Ca2+ to bind is similar to the affinity of αsl-casein for the same binding event: however, binding of subsequent Ca2+ to β-casein is weaker than the binding to αs1-casein. The results are discussed in terms of precipitability of the 2 caseins caused by the binding of Ca2+.

Type
Original Articles
Information
Journal of Dairy Research , Volume 48 , Issue 1 , February 1981 , pp. 71 - 76
Copyright
Copyright © Proprietors of Journal of Dairy Research 1981

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References

REFERENCES

Annan, W. D. & Manson, W. (1969). Journal of Dairy Research 36, 259–268.CrossRefGoogle Scholar
Dalgleish, D. G. & Parker, T. G. (1979). Journal of Dairy Research 46, 259–263.CrossRefGoogle Scholar
Dalglkish, D. G. & Parker, T. G. (1980). Journal of Dairy Research 47, 113–122.CrossRefGoogle Scholar
Dickson, I. R. & Perkins, D. J. (1971). Biochemical Journal 124, 235–240.CrossRefGoogle Scholar
Grizzuti, K. & Perlmann, G. E. (1973). Biochemistry 12, 4399–4403.CrossRefGoogle Scholar
Grosclaude, F., Mahé, M. F. & Ribadeau-Dumas, B. (1973). European Journal of Biochemistry 40, 323–324.CrossRefGoogle Scholar
Horne, D. S. & Dalgleish, D. G. (1980). International Journal of Biological Macromolecules 2, 154–160.CrossRefGoogle Scholar
Manson, W. & Annan, W. D. (1971). Archives of Biochemistry and Biophysics 145, 16–26.CrossRefGoogle Scholar
Mercier, J. -C, Grosclaude, F. & Ribadeau-Dumas, B. (1971). European Journal of Biochemistry 23, 41–51.CrossRefGoogle Scholar
Ribadeau-Dumas, B., Brignon, G., Grosclaude, F. & Mercier, J. -C. (1972). European Journal of Biochemistry 25, 505–514.CrossRefGoogle Scholar
Slattery, C. W. (1975). Biophysical Chemistry 3, 83–89.CrossRefGoogle Scholar
Slattery, C. W. & Waugh, D. F. (1973). Biophysical Chemistry 1, 104–111.CrossRefGoogle Scholar
Waugh, D. F., Slattery, C. W. & Creamer, L. K. (1971). Biochemistry 10, 817–823.CrossRefGoogle Scholar
Zittle, C. A. & Custer, J. H. (1963). Journal of Dairy Science 46, 1183–1188.CrossRefGoogle Scholar