AbstractThe interaction of myelin basic protein (MBP) from bovine central nervous system with divalent zinc ion was studied by UV‐Vis titration spectrophotometry and isothermal titration calorimetry techniques at 27°C in Tris buffer solution at pH = 7.2. MBP has one binding site for a zinc ion. The binding of a zinc ion is endothermic (ΔH = + 159 kJ mol−1) with a dissociation binding constant of 0.445 μM. The results obtained by two previous methods of isothermal titration spectrophotometry and calorimetry are similar and consistent with the result obtained from a new calculation method of calorimetric data analysis according to the Scatchard plot.
