These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: In vitro binding of 3,4,5,6-tetrachloro-1,2-benzoquinone by rat liver glutathione S-transferases.
    Author: Dierickx PJ.
    Journal: Res Commun Chem Pathol Pharmacol; 1983 Sep; 41(3):517-20. PubMed ID: 6635333.
    Abstract:
    The in vitro interaction of 3,4,5,6-tetrachloro-1,2-benzoquinone (o-chloranil) with rat liver glutathione S-transferases (GST) was studied, using reduced glutathione (GSH) and 1-chloro-2,4-dinitrobenzene (CDNB) as substrates. o-Chloranil inhibited the GST activity in crude extracts in a dose dependent manner, while 3,6-dichloro-2,5-dihydroxy-1,4-benzoquinone did not. Each of the GST isoenzymes was inhibited, albeit at 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 indicated a minor spontaneous conjugation of o-chloranil with GSH, which was not enzymatically activated. It is concluded that o-chloranil interact with GST by direct binding to these proteins. This binding could have a protective function against o-chloranil.
    [Abstract] [Full Text] [Related] [New Search]