Thermodynamic Study of the Binding of Mercury Ion to Human Growth Hormone at Different Temperatures

Abstract

The interaction of human growth hormone (hGH) with the divalent mercury ion was studied by isothermal titration calorimetry at two temperatures of 27 °C and 37 °C in aqueous solutions. We found that there is a set of two identical and non-interacting binding sites for Hg2+ ions. The intrinsic dissociation equilibrium constant and the molar enthalpy of binding are 4.2 mmol⋅L−1 and −14.8 kJ⋅mol−1 at 27 °C and 5.1 mmol⋅L−1 and −14.2 kJ⋅mol−1 at 37 °C, respectively. The results obtained indicate that the stability of the protein increases due to the binding of mercury ions using the extended solvation theory.