Acetaldehyde-dependent oxidation of glutathione catalyzed by rat liver cytosol.

Abstract:

:We have identified a novel reaction in which acetaldehyde promotes rat hepatic cytosolic catalysis of O2 consumption coupled with glutathione oxidation without apparent release of activated forms of O2. Acetaldehyde is not consumed in the reaction. The reaction (O2 consumption or oxidized glutathione production) is saturable with respect to varying glutathione (K'm congruent to 20-45 microM) but not at high acetaldehyde concentrations. However, activity in the range of acetaldehyde found in liver from alcohol metabolism (10-100 microM) appeared to be saturable (K'm congruent to 25-50 microM). Since neither acetaldehyde-dependent glutathione loss nor O2 consumption is detectable in guinea pig hepatic cytosol or hepatic cytosol from selenium-deficient rats, we propose that acetaldehyde interacts with glutathione peroxidase, converting the enzyme into a glutathione oxidase.

authors

Lyon I,Kaplowitz N

doi

10.1016/0006-291x(85)91983-7

subject

Has Abstract

pub_date

1985-06-28 00:00:00

pages

949-57

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(85)91983-7

journal_volume

129

pub_type

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