Literature DB >> 7264011

Binding of calcium ions to bovine beta-casein.

T G Parker, D G Dalgleish.   

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+.

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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


  2 in total

1.  Intraluminal chemistry of zinc in milks.

Authors:  J G Brushmiller; R W Ames; F A Jacobs; L S Nelson
Journal:  Biol Trace Elem Res       Date:  1989 Jan-Feb       Impact factor: 3.738

2.  Calcium-induced associations of the caseins: thermodynamic linkage of calcium binding to colloidal stability of casein micelles.

Authors:  T F Kumosinski; H M Farrell
Journal:  J Protein Chem       Date:  1991-02
  2 in total

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