Interaction of anticancer drugs with human and bovine serum albumin

被引：98

作者：

Sulkowska, A

Równicka, J

Bojko, B

Sulkowski, W

机构：

[1] Med Univ Silesia, Dept Phys Pharm, PL-41200 Sosnowiec, Poland

[2] Silesian Univ, Dept Environm Chem & Technol, PL-40006 Katowice, Poland

来源：

JOURNAL OF MOLECULAR STRUCTURE | 2003年 / 651卷

关键词：

allopurinol-mercaptopurine binding; binding stoichiometry; fluorescence quenching;

D O I：

10.1016/S0022-2860(02)00642-7

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 properties of 5-fluorouracil (5FU), 6-azauracil (6AU), 6-mercaptopurine (6MP), thiouracil (2TU) and thioimidazole (TI), as a quencher of fluorescence of tryptophanyl Trp 214 residue in serum albumin were studied. For the molar ratio [ligand]: [BSA] = 30: 1 the decrease of protein fluorescence due to the presence of thiouracil as a quencher attains 90%, while imidazole derivative-thiamazole quenches the BSA fluorescence only by 25%. To estimate the character of the binding between studied quencher and human and bovine serum albumin the Scatchard. and Stern-Volmer methods were used. The binding stoichiometry of allopurinol -mercaptopurine -serum albumin complex was studied. (C) 2003 Elsevier Science B.V. All rights reserved.

引用

页码：133 / 140

页数：8

共 15 条

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BROOKS RJ, 1982, BIOMED PHARMACOTHER, V36, P217

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