Application of the extended solvation model for thermodynamic study of copper ion binding to Jack bean urease

作者：Behbehani G Rezaei^*; Saboury A A; Poorakbar E; Barzegar L

来源：Journal of Thermal Analysis and Calorimetry, 2010, 102(3): 1141-1146.

DOI：10.1007/s10973-010-0842-5

• Jack bean urease
• Isothermal titration calorimetry
• Inhibitor
• Binding parameters

A Thermodynamic study on the interaction Jack bean urease, JBU, with Cu(2+) ion was studied by isothermal titration calorimetry (ITC) at 300 and 310 K in 30 mM Tris buffer solution, pH 7.0. The heats of JBU + Cu(2+) interactions are reported and analyzed in terms of the extended solvation theory. It was indicated that there are a set of 12 identical and non-cooperative sites for Cu(2+) ion. The binding of Cu(2+) ion with JBU is exothermic with dissociation equilibrium constants of 284.883 and 345.855 mu M at 300 and 310 K, respectively.

• 出版日期2010-12