A Thermodynamic Study on the Binding of Cobalt Ion with Myelin Basic Protein

Bulletin of the Korean chemical society

A. Fallah Baghery¹  A. A. Saboury¹  G. Rezaei Behbehani¹ 

关键词: Myelin basic protein;    Cobalt;    Isothermal titration calorimtry;    Solvation parameters;   

DOI  :  

学科分类：化学（综合）

来源: Korean Chemical Society

【 摘 要 】

The interaction of myelin basic protein (MBP) from bovine central nervous system with divalent calcium ion was studied by isothermal titration calorimetry at 27�? in aqueous solution. The extended solvation model was used to reproduce the enthalpies of Co²⁺-MBP interaction over the whole Co²⁺ concentrations. The solvation parameters recovered from the solvation model were attributed to the structural change of MBP due to the metal ion interaction. It was found that there is a set of three identical and noninteracting binding sites for Co²⁺ ions. The association equilibrium constant is 0.015 レM^?1. The molar enthalpy of binding is ツH = ?14.60 kJ mol^?1.

【 授权许可】

Unknown