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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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