A thermodynamic study on the interaction of nickel ion with myelin basic protein by isothermal titration calorimetry |
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Authors: | G Rezaei Behbehani A A Saboury L Barzegar O Zarean J Abedini M Payehghdr |
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Institution: | (1) Chemistry Department, Imam Khomeini International University, Qazvin, Iran;(2) Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran;(3) Chemistry Department, Payam Noor University (PNU), Abhar, Iran;(4) Chemistry Department, Payam Noor University (PNU), Karaj, Iran |
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Abstract: | The interaction of myelin basic protein (MBP) from the bovine central nervous system with divalent nickel ion was studied
by isothermal titration calorimetry at 37 and 47 °C in Tris buffer solution at pH = 7. The new solvation model was used to
reproduce the heats of MBP + Ni2+ interaction over the whole Ni2+ concentrations. It was found that MBP has three identical and independent binding sites for Ni2+ ions. The intrinsic dissociation equilibrium constant and the molar enthalpy of binding are 89.953 μM, −14.403 kJ mol−1 and 106.978 μM, −14.026 kJ mol−1 at 37 and 47 °C, respectively. The binding parameters recovered from the new solvation model were correlated to the structural
changes of MBP due to its interaction with nickel ion interaction. It was found that in the low and high concentrations of
the nickel ions, the MBP structure was destabilized. |
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