Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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A Thermodynamic Study on the Binding of Cobalt Ion with Myelin Basic Protein

  • Behbehani, G. Rezaei (Chemistry Department, Imam Khomeini International University) ;
  • Saboury, A.A. (Institute of Biochemistry and Biophysics, University of Tehran) ;
  • Baghery, A. Fallah (Chemistry Department, Imam Khomeini International University)
  • Published : 2008.04.20
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Abstract

The interaction of myelin basic protein (MBP) from bovine central nervous system with divalent calcium ion was studied by isothermal titration calorimetry at 27 ${^{\circ}C}$ in aqueous solution. The extended solvation model was used to reproduce the enthalpies of $Co^{2+}$-MBP interaction over the whole $Co^{2+}$ 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 $Co^{2+}$ ions. The association equilibrium constant is 0.015 ${\mu}M^{-1}$. The molar enthalpy of binding is $\Delta$H = −14.60 kJ $mol^{-1}$.

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