In vitro binding of acetic acid and its chlorinated derivatives by the soluble glutathione S-transferases from rat liver.
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.
D000085:Acetates / Q000378:metabolism / Q000494:pharmacology*; D019342:Acetic Acid; D000818:Animals; D003999:Dichloroacetic Acid / Q000378:metabolism / Q000494:pharmacology*; D005982:Glutathione Transferase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000037:antagonists & inhibitors* / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D011485:Protein Binding; D051381:Rats; D014238:Trichloroacetic Acid / Q000378:metabolism / Q000494:pharmacology*
D000085:Acetates; D007527:Isoenzymes; C006972:chloroacetic acid; D014238:Trichloroacetic Acid; D003999:Dichloroacetic Acid; D005982:Glutathione Transferase; D019342:Acetic Acid