| Literature DB >> 7264011 |
Abstract
The isotherms for Ca++ binding to bovine alpha-casein have been measured at 5 temperatures in the range 4-40 degrees 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 alpha s1-casein. The affinity of beta-casein for the first Va2+ to bind is similar to the affinity of alpha s1-casein for the same binding event: however, binding of subsequent Ca2+ to beta-casein is weaker than the binding to alpha s1-casein. The results are discussed in terms of precipitability of the 2 caseins caused by the binding of Ca2+.Entities:
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Year: 1981 PMID: 7264011 DOI: 10.1017/s0022029900021476
Source DB: PubMed Journal: J Dairy Res ISSN: 0022-0299 Impact factor: 1.904