Studies on the reaction between zincon and bovine serum albumin

被引：0

作者：

Chi, YH

Zhuang, J

Li, N

Li, KA ^{[1
]}

Tong, SY

机构：

[1] SW Inst Technol, Dept Mat Sci & Engn, Mianyang 621002, Peoples R China

[2] Peking Univ, Coll Chem & Mol Engn, Beijing 100871, Peoples R China

来源：

CHEMICAL JOURNAL OF CHINESE UNIVERSITIES-CHINESE | 1999年 / 20卷 / 11期

关键词：

zincon; bovine serum albumin; UV spectra; apparent binding equilibricem constant; denaturant;

D O I：

暂无

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The interaction of zincon (ZCN) with bovine serum albumin (BSA) and the changes of its spectrum were studied by UV spectra at pH 4. 1 buffer solution. The conditional constants, apparent molar absorptivity epsilon(p) = 1. 3 X 10(6) L . mol(-1) . cm(-1), maximum binding number n = 278 and apparent binding equilibrium constant K-c = 8 X 10(7) were obtained, It was considered that electrostatic force is the main binding force. The ion(sodium chloride) concentration of the solution has significant effect on binding reaction of BSA and ZCN, The effects of different denaturants were also examined. The Scatchard model is appropriate in the treatment of data, obtained.

引用

页码：1697 / 1702

页数：6

共 11 条

[1]

Chi YH, 1998, CHEM J CHINESE U, V19, P879

[2] THE BINDING INTERACTION OF COOMASSIE BLUE WITH PROTEINS [J].