Abstract
The interaction of myelin basic protein with Nickel ions was studied by Isothermal Titration Calorimetry (ITC) at in tris buffer, pH=7. The enthalpies of MBP+Ni2+interaction are reported and analysed in term of the new solvation theory. It was found that MBP has three identical and cooperative binding sites for Ni2+ions. The dissociation equilibrium constant and the molar enthalpy of binding are 75.015 µM, -14.815 kJmol-1. The binding parameters recovered from the new equation, attributed to the structural change of MBP and its biological activity due to metal ion interaction. The binding of nickel ions cause some changes in stability of MBP at low and high Ni2+concentrations.
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