Studies on the interaction between mytomycin C and bovine serum albumin

被引：0

作者：

Yi, PG ^{[1
]}

Shang, ZC

Yu, XS

Shao, S

Lin, RS

机构：

[1] Zhejiang Univ, Dept Chem, Hangzhou 310027, Peoples R China

[2] Xiangtan Polytech Univ, Dept Chem Engn, Xiangtan 411201, Peoples R China

来源：

ACTA CHIMICA SINICA | 2000年 / 58卷 / 12期

关键词：

mytomycin C; bovine serum albumin; fluorescence; microcalorimetry;

D O I：

暂无

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The binding characteristics of mytomycin C (MMC) with bovine serum albumin (BSA) have been studied by fluorescence spectsoscopy and microcalorimetry method in aqueous solution. The equilibrium constant KA, the number of binding sites n, and the thermodynamic functions for the reaction have all been measured. The binding distance between MMC and BSA and the transfer efficiency have been obtained based on the mechanism of Forster energy transfer. The effect of MMC on the conformation of BSA has also been analyzed using synchronous fluorescence spectroscopy.

引用

页码：1649 / 1653

页数：5

共 16 条

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