A Novel method for Thermodynamic Study on the Binding of Milk Carrier protein of BLG-A with Cr+3

G. Behbehania; A. Divsalar; A. Saboury

doi:10.2478/v10026-009-0039-5

Abstract

Thermodynamics of the interaction between Cr³⁺ with β-lactoglobulin type A (BLG-A) was investigated at pH 7.0 and 37°C by isothermal titration calorimetry. A new method to follow the effect of Cr³⁺ on the stability of BLG-A was introduced. The new solvation model was used to reproduce the enthalpies of BLG-A+ Cr³⁺ interactions over the whole range of Cr³⁺ concentrations. The solvation parameters recovered from the new equation are attributed to the structural change of BLG-A and its biological activity. The results obtained indicate that there is a set of two identical binding sites for Cr³⁺ ions with positive cooperativity. The association equilibrium constants are 14.39 and 0.49 mM^-1 for the first and second binding site, respectively. The enthalpy of binding for one mole of Cr⁺³ ion to one mole of the binding site on BLG-A (ΔH=104.60 kJ mol^-1) is obtained.

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A Novel method for Thermodynamic Study on the Binding of Milk Carrier protein of BLG-A with Cr+3

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