A new approach for titration calorimetric data analysis on the binding of magnesium ion with myelin basic protein

被引：7

作者：

Behbehani, G. Rezaei ^{[1
]}

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

Baghery, A. Fallah ^{[2
]}

机构：

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

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

来源：

JOURNAL OF SOLUTION CHEMISTRY | 2008年 / 37卷 / 08期

基金：

美国国家科学基金会;

关键词：

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

D O I：

10.1007/s10953-008-9297-8

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The interaction of the myelin basic protein (MBP) from the bovine central nervous system with divalent magnesium ion was studied by isothermal titration calorimetry at 27 degrees C in aqueous solution. A simple rapid method for determination of the dissociation binding constants for Mg2+-MBP interaction was introduced using the isothermal titration calometric data. The binding isotherm for Mg2+-MBP interaction is easily obtained by carrying out a titration calorimetric experiment using only one set of concentrations of MBP. There are two identical independent intrinsic association constants equal to 0.021 mu mol.L-1 in the first- and second-binding sites, respectively.

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页码：1127 / 1135

页数：9

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