Abstract
The interaction of the myelin basic protein (MBP) from the bovine central nervous system with divalent magnesium ion was studied by isothermal titration calorimetry at 27 °C in aqueous solution. A simple rapid method for determination of the dissociation binding constants for Mg2+-MBP interaction was introduced using the isothermal titration calometric data. The binding isotherm for Mg2+-MBP interaction is easily obtained by carrying out a titration calorimetric experiment using only one set of concentrations of MBP. There are two identical independent intrinsic association constants equal to 0.021 μmol⋅L−1 in the first- and second-binding sites, respectively.
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