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

被引：4

作者：

Behbehani, G. Rezaei ^{[1
]}

Saboury, A. A. ^{[2
]}

Poorakbar, E. ^{[2
,3
]}

Barzegar, L. ^{[1
]}

机构：

[1] Imam Khomeini Int Univ, Dept Chem, Qazvin, Iran

[2] Univ Tehran, Inst Biochem & Biophys, Tehran, Iran

[3] Payam Noor Univ, Dept Biol, Tehran, Iran

来源：

JOURNAL OF THERMAL ANALYSIS AND CALORIMETRY | 2010年 / 102卷 / 03期

关键词：

Jack bean urease; Isothermal titration calorimetry; Inhibitor; Binding parameters; HIGH-PERFORMANCE METHOD; INHIBITION; LYSOZYME; ENTHALPY;

D O I：

10.1007/s10973-010-0842-5

中图分类号：

O414.1 [热力学];

学科分类号：

摘要：

A Thermodynamic study on the interaction Jack bean urease, JBU, with Cu2+ 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 + Cu2+ 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 Cu2+ ion. The binding of Cu2+ ion with JBU is exothermic with dissociation equilibrium constants of 284.883 and 345.855 mu M at 300 and 310 K, respectively.

引用

收藏

页码：1141 / 1146

页数：6

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