A thermodynamic investigation on the binding of mercury ion with myelin basic protein at different temperatures

Abstract

Abstract A thermodynamic study on the interaction of myelin basic protein with mercury ion was studied by using isothermal titration calorimetry, ITC, at 300.15, 310.15 and 320.15 K in Tris buffer solution at pH 7. The enthalpies of MBP + Hg 2+ interaction are reported and analysed in terms of the extended solvation model. It was found that MBP has two identical and non-cooperative binding sites for Hg 2+ ions. The intrinsic dissociation equilibrium constants are 99.904, 112.968 and 126.724 μmol/L, and the molar enthalpy of binding are −11.634, −10.768 and −10.117 kJ mol −1 at 300.15, 310.15 and 320.15 K, respectively.