<abstract xml:lang="en" xmlns="http://www.w3.org/1999/xhtml">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.</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.

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

Chemistry department, Imam Khomeini International University, Qazvin, Iran

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

Department of Biological Sciences, Tarbiat Moollem University, Tehran, Iran

Polish Journal of Chemical Technology

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

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...

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

Pubblicato online: 08 gen 2010

Pagine: 24 - 29

DOI: https://doi.org/10.2478/v10026-009-0039-5

Parole chiave
BLG-A, Cr, isothermal titration calorimetry, binding parameters

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