DIFFERENTIAL ACTIVITY OF HUMAN, RAT, MOUSE AND BACTERIA GLUTATHIONE TRANSFERASE ISOENZYMES TOWARDS 4-NITROQUINOLINE 1-OXIDE

被引：32

作者：

ACETO, A ^{[1
]}

DIILIO, C ^{[1
]}

LOBELLO, M ^{[1
]}

BUCCIARELLI, T ^{[1
]}

ANGELUCCI, S ^{[1
]}

FEDERICI, G ^{[1
]}

机构：

[1] UNIV ROMA TOR VERGATA,DIPARTIMENTO BIOL,I-00190 ROME,ITALY

来源：

CARCINOGENESIS | 1990年 / 11卷 / 12期

关键词：

D O I：

10.1093/carcin/11.12.2267

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

The conjugation capacity of 4-nitroquinoline 1-oxide (4-NQO) with GSH by a number of human, rat, mouse and bacteria glutathione transferases (GSTs) was investigated. Pi and mu classes GSTs exhibited maximum conjugation capacity. Alpha class glutathione transferases as well as bacteria glutathione transferases were found to be unable to conjugate GSH to 4-NQO. The K(m) values as well as the catalytic efficiency (K(cat)/K(m)) for most of the GSTs investigated were also determined. Mouse liver GST MIII (class mu) was the most efficient of the various isoenzymes tested. Its K(cat)/K(m) value was 162 times higher than that of mouse liver GST MI (class alpha). The relatively high catalytic efficiency exhibited by GST-pi-(class pi) is prevalently due to its low affinity for 4-NQO.

引用

页码：2267 / 2269

页数：3

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