No abstract

Mercury ion interaction with myelin basic protein (MBP) was studied at 300 K in 30 mmol/L tris buffer, pH＝7 by isothermal titration calorimetry (ITC). An extended solvation model was used for Hg 2＋ ＋MBP interaction over the whole range of Hg 2＋ concentrations. The binding parameters recovered from the solvation model were attributed to the structural changes of MBP due to its interaction with mercury ion. It was found that mercury ion acted as a noncooperative effector of MBP, and there is a set of two identical and independent binding sites for Hg 2＋ ions.The dissociation equilibrium constant is 97.6 µmol/L. The molar enthalpy change of binding is -11.25 kJ•mol -1 .