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A Thermodynamic Study on the Binding of Calcium Ion with Myelin Basic Protein

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Abstract

The interaction of myelin basic protein (MBP) from the bovine central nervous system with divalent calcium ion was studied by isothermal titration calorimetry at 27 °C in aqueous solution. The extended solvation model was used to reproduce the enthalpies of Ca2+-MBP interaction over the whole range of Ca2+ 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 two identical and non-interacting binding sites for Ca2+ ions. The association equilibrium constant is 0.021 μmol⋅dm−3. The molar enthalpy of binding is ΔH=−15.10 kJ⋅mol−1.

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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

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

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Behbehani, G.R., Saboury, A.A. & Baghery, A.F. A Thermodynamic Study on the Binding of Calcium Ion with Myelin Basic Protein. J Solution Chem 36, 1311–1320 (2007). https://doi.org/10.1007/s10953-007-9181-y

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  • DOI: https://doi.org/10.1007/s10953-007-9181-y

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