Application of an extended solvation theory to study on the binding of magnesium ion with myelin basic protein

被引：18

作者：

Behbehani, G. Rezaei ^{[1
]}

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

Baghery, A. Fallah ^{[1
]}

Abedini, A. ^{[3
]}

机构：

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

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

[3] Payam Noor Univ, Dept Chem, Abhar, Iran

来源：

JOURNAL OF THERMAL ANALYSIS AND CALORIMETRY | 2008年 / 93卷 / 02期

基金：

美国国家科学基金会;

关键词：

isothermal titration calorimetry; magnesium; myelin basic protein; solvation parameters;

D O I：

10.1007/s10973-007-8674-7

中图分类号：

O414.1 [热力学];

学科分类号：

摘要：

Binding properties of myelin basic protein (MBP) from bovine central nervous system due to the interaction by divalent magnesium ion (Mg2+) was investigated at 27 degrees C in aqueous solution using isothermal titration calorimetry (ITC) technique. An extended solvation model was used to reproduce the enthalpies of Mg2+-MBP interaction over the whole Mg2+ concentrations. It was found that there is a set of two identical and noninteracting binding sites for Mg2+ ions. The dissociation equilibrium constant is K-d=45.5 mu M. The molar enthalpy of binding site is identical for both sites; Delta H= -15.24 kJ mol(-1). The solvation parameters recovered from the solvation model were attributed to the structural change of MBP due to the metal ion interaction.

引用

页码：479 / 483

页数：5

共 40 条

[1] Enthalpy and enzyme activity of modified histidine residues of adenosine deaminase and diethyl pyrocarbonate complexes [J].