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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 29, Number 4
BKCSDE 29(4)
April 20, 2008 

A Thermodynamic Study on the Binding of Cobalt Ion with Myelin Basic Protein
G. Rezaei Behbehani*, A. A. Saboury, A. Fallah Baghery
Myelin basic protein, Cobalt, Isothermal titration calorimtry, Solvation parameters
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 μM?1. The molar enthalpy of binding is ΔH = ?14.60 kJ mol?1.
736 - 740
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