A NOVEL NADPH NADH-DEPENDENT ALDEHYDE REDUCTION ENZYME ISOLATED FROM THE TAPEWORM MONIEZIA-EXPANSA

被引：5

作者：

BROPHY, PM ^{[1
]}

CROWLEY, P ^{[1
]}

BARRETT, J ^{[1
]}

机构：

[1] UNIV COLL ABERYSTWYTH,DEPT BIOL SCI,ABERYSTWYTH SY23 3DA,DYFED,WALES

来源：

FEBS LETTERS | 1990年 / 263卷 / 02期

基金：

英国医学研究理事会;

关键词：

(Moniezia expansa); Alcohol dehydrogenase; Aldehyde reductase; Lipid peroxidation;

D O I：

10.1016/0014-5793(90)81400-I

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

An aldehyde reduction enzyme has been purified from the cytosol of the tapeworm, Moniezia expansa, by chromatofocusing and Reactive-Red chromatography. The enzyme is monomeric (subunit 34 kDa) and can utilise NADH and NADPH as co-factors. Substrates of the enzyme include alkanals, alka-2,4-dienals and alk-2-enals, established secondary products of lipid peroxidation. The enzyme reduced methylglyoxal, another possible natural substrate (M. expansa lacks glyoxalase I activity). The parasite enzyme may help form a final line of defence against cytotoxic aldehydes arising from host immune initiated lipid peroxidation. © 1990.

引用

页码：305 / 307

页数：3

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