A novel NADPH/NADH‐dependent aldehyde reduction enzyme isolated from the tapeworm Moniezia expansa
- 24 April 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 263 (2) , 305-307
- https://doi.org/10.1016/0014-5793(90)81400-i
Abstract
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.Keywords
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