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

• Authors: G. Behbehania , A. Divsalar , A. Saboury
• Languages of publication: EN

Abstracts

EN

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.

Keywords

EN

BLG-A; Cr+3; isothermal titration calorimetry; binding parameters

• Publisher: De Gruyter Open
• Journal: Polish Journal of Chemical Technology
• Year: 2009
• Volume: 11
• Issue: 4
• Pages: 24-29

Dates

published

1 - 1 - 2009

online

8 - 1 - 2010

Contributors

author

G. Behbehania

• Chemistry department, Imam Khomeini International University, Qazvin, Iran

author

A. Divsalar

author

A. Saboury

• Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

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Identifiers

DOI

10.2478/v10026-009-0039-5