Inactivation by gallic acid of cytosolic aconitase extracted from rat liver

被引：2

作者：

Iwata, S ^{[1
]}

Murakami, K ^{[1
]}

Haneda, M ^{[1
]}

Yoshino, M ^{[1
]}

机构：

[1] Aichi Med Univ, Dept Biochem, Aichi 4801195, Japan

来源：

BIOMEDICAL RESEARCH-TOKYO | 1999年 / 20卷 / 02期

关键词：

D O I：

10.2220/biomedres.20.81

中图分类号：

R-3 [医学研究方法]; R3 [基础医学];

学科分类号：

1001 [基础医学];

摘要：

Inactivation by gallic acid derivatives of cytosolic aconitase from rat liver was analyzed. Cytosolic aconitase was effectively and preferentially inactivated by treatment with gallic acid, which did not affect fumarase, NADP-isocitrate dehydrogenase, malic enzyme, tryptophan dioxygenase, and xanthine oxidase. However, pyrogallol and alkylgallates such as ethyl-, butyl-, octyl- and laurylgallates did not inactivate aconitase. Gallic acid enhanced autooxidation of Fe2+ ion, but alkylgallates did not. Spectrophotometric analyses revealed that gallic acid is irreversibly modified by a transition metal such as copper, but alkylated gallic acids showed only the metal-chelating activity. Gallic acid composed of a pyrogallol moiety and a carboxyl group binds to aconitase, and can inactivate the enzyme by oxidizing iron-sulfur cluster at the active site. The inactivation of aconitase by gallic acid may participate in the well-known cytotoxicity of this compound.

引用

页码：81 / 86

页数：6

共 22 条

[1]

ACONITASE, A 2-FACED PROTEIN - ENZYME AND IRON REGULATORY FACTOR [J].