Competing binding of metal ions with protein studied by microdialysis

被引：4

作者：

Guo, M

Kong, L

Mao, XQ

Li, X

Zou, HF ^{[1
]}

机构：

[1] Acad Sinica, Dalian Inst Chem Phys, Natl Chromatog R&D Ctr, Dalian 116011, Peoples R China

[2] Dalian Univ, Dept Chem & Chem Technol, Dalian 116622, Peoples R China

来源：

SCIENCE IN CHINA SERIES B-CHEMISTRY | 2002年 / 45卷 / 02期

关键词：

microdialysis; high performance liquid chromatography; human serum albumin; metal ions; competing binding;

D O I：

10.1360/02yb9021

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A method has been established to study the competing binding of metal ions with protein by a combined technique of microdialysis with high performance liquid chromatography (HPLC). Ni2+, Cd2+, Zn2+, Cu2+ and human serum albumin (HSA) were chosen as model metal ions and protein. The experimental results show that Ni2+ and Cu2+ share a common primary binding site on HSA, and Zn2+ and Cd2+ share a different common primary binding site from them, but there is a common multi-metal binding site for all of those four metal ions. This method show advantages of fast sampling, easily to be operated and especially to be useful when ideal spectroscopic probes are not available for the study of interaction between protein and metal ions.

引用

收藏

页码：151 / 157

页数：7

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