Citation: G. Rezaei Behbehani, L. Barzegar, A. A. Saboury, S. Ghammami. A thermodynamic investigation on the binding of mercury ion with myelin basic protein at different temperatures[J]. Chinese Chemical Letters, ;2011, 22(5): 623-625. doi: 10.1016/j.cclet.2010.11.028 shu

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

a Chemistry Department, Faculty of Science, Islamic Azad University, Takestan Branch, Takestan, Iran;
b Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran;
c Department of Chemistry, Imam Khomeini International University, Qazvin, Iran

Received Date: 23 July 2010

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+Hg²⁺ 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 Hg²⁺ 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.
- Myelin basic protein,
- Mercury ion,
- Isothermal titration calorimtry,
- Binding parameters
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