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Application of an extended solvation theory to study on the binding of magnesium ion with myelin basic protein

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Abstract

Binding properties of myelin basic protein (MBP) from bovine central nervous system due to the interaction by divalent magnesium ion (Mg2+) was investigated at 27°C in aqueous solution using isothermal titration calorimetry (ITC) technique. An extended solvation model was used to reproduce the enthalpies of Mg2+-MBP interaction over the whole Mg2+ concentrations. It was found that there is a set of two identical and noninteracting binding sites for Mg2+ ions. The dissociation equilibrium constant is K d=45.5 μM. The molar enthalpy of binding site is identical for both sites; ΔH=−15.24 kJ mol−1. The solvation parameters recovered from the solvation model were attributed to the structural change of MBP due to the metal ion interaction.

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Authors and Affiliations

  1. Chemistry Department, Imam Khomeini International University, Qazvin, Iran

    G. Rezaei Behbehani & A. Fallah Baghery

  2. Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

    A. A. Saboury

  3. Chemistry Department, Payam Noor University, Abhar, Iran

    A. Abedini

Authors
  1. G. Rezaei Behbehani
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  2. A. A. Saboury
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  3. A. Fallah Baghery
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  4. A. Abedini
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Correspondence to G. Rezaei Behbehani.

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Rezaei Behbehani, G., Saboury, A.A., Fallah Baghery, A. et al. Application of an extended solvation theory to study on the binding of magnesium ion with myelin basic protein. J Therm Anal Calorim 93, 479–483 (2008). https://doi.org/10.1007/s10973-007-8674-7

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  • DOI: https://doi.org/10.1007/s10973-007-8674-7

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