Abstract
SummaryThe 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+.
References
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Dates
Type | When |
---|---|
Created | 16 years, 2 months ago (June 5, 2009, 3:03 a.m.) |
Deposited | 6 years, 3 months ago (May 25, 2019, 12:46 p.m.) |
Indexed | 11 months, 2 weeks ago (Sept. 7, 2024, 2 a.m.) |
Issued | 44 years, 6 months ago (Feb. 1, 1981) |
Published | 44 years, 6 months ago (Feb. 1, 1981) |
Published Online | 16 years, 2 months ago (June 1, 2009) |
Published Print | 44 years, 6 months ago (Feb. 1, 1981) |
@article{Parker_1981, title={Binding of calcium ions to bovine β-casein}, volume={48}, ISSN={1469-7629}, url={http://dx.doi.org/10.1017/s0022029900021476}, DOI={10.1017/s0022029900021476}, number={1}, journal={Journal of Dairy Research}, publisher={Cambridge University Press (CUP)}, author={Parker, Thomas G. and Dalgleish, Douglas G.}, year={1981}, month=feb, pages={71–76} }