Rat glutathione transferase 8-8, an enzyme efficiently detoxifying 4-hydroxyalk-2-enals.

Abstract:

:Rat glutathione transferase 8-8 is one of the less abundant cytosolic glutathione transferases, accounting for approx. 1% of the total activity with 1-chloro-2,4-dinitrobenzene in liver. The enzyme is eluted at pH 6.3 upon chromatofocusing and has so far been identified in liver, kidney, lung and testis. Characteristic properties include high relative activity with ethacrynic acid (70% of the specific activity with 1-chloro-2,4-dinitrobenzene) and an apparent subunit Mr of 24 500. The most significant property noted is the high catalytic activity in the conjugation of 4-hydroxyalk-2-enals, major products of lipid peroxidation. The catalytic efficiency with these substrates exceeds corresponding values for all known substrates tested with any glutathione transferase, which suggests that transferase 8-8 may have evolved to detoxify 4-hydroxyalk-2-enals.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Jensson H,Guthenberg C,Alin P,Mannervik B

doi

10.1016/0014-5793(86)80743-8

subject

Has Abstract

pub_date

1986-07-28 00:00:00

pages

207-9

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(86)80743-8

journal_volume

203

pub_type

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