In vitro binding of acetic acid and its chlorinated derivatives by the soluble glutathione S-transferases from rat liver

Dierickx, PJ

HERO ID

2301041

Reference Type

Journal Article

Year

1984

Language

English

PMID

6739960

HERO ID 2301041
In Press No
Year 1984
Title In vitro binding of acetic acid and its chlorinated derivatives by the soluble glutathione S-transferases from rat liver
Authors Dierickx, PJ
Journal Research Communications in Chemical Pathology and Pharmacology
Volume 44
Issue 2
Page Numbers 327-330
Abstract The in vitro interaction of acetic acid and its chlorinated derivatives with rat liver glutathione S-transferases (GST) was studied, using glutathione (GSH) and 1-chloro-2,4-dinitrobenzene (CDNB) as substrates. The investigated compounds inhibited the GST activity in crude extracts in a dose dependent manner. Each of the different GST isoenzymes was inhibited by each of the compounds under study, albeit at very different degrees. Kinetic studies never revealed competitive inhibition kinetics, with GSH nor CDNB as the variable substrate. Titration of remaining GSH in appropriate incubation mixtures revealed no GST catalyzed conjugation with GSH. It is concluded that acetic acid and its chlorinated derivatives interact with GST by direct binding to these proteins. This binding could have a protective function against these compounds.
Pmid 6739960
Is Certified Translation No
Dupe Override No
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Is Public Yes
Language Text English