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Indomethacin inhibition of glutathione S-transferases

dc.contributor.authorWu, Chungen_US
dc.contributor.authorMathews, Kenneth P.en_US
dc.date.accessioned2006-04-07T18:42:35Z
dc.date.available2006-04-07T18:42:35Z
dc.date.issued1983-05-16en_US
dc.identifier.citationWu, Chung, Mathews, Kenneth P. (1983/05/16)."Indomethacin inhibition of glutathione S-transferases." Biochemical and Biophysical Research Communications 112(3): 980-985. <http://hdl.handle.net/2027.42/25218>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WBK-4DP5MPT-4J/2/dd0297c67193ffa22f7558d9bca90222en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/25218
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6847692&dopt=citationen_US
dc.description.abstractIndomethacin inhibited rat liver glutathione S-transferases (EC 2.5.1.18). Its inhibition was non-competitive with respect to 3,4-dichloronitrobenzene with an apparent Ki of 5.3 x 10-5 M and uncompetitive with respect to glutathione with an apparent Ki of 4.0 x 10-5 M. 4-Chlorobenzoic acid and 5-methoxy-2-methylindole-3-acetic acid, two metabolites of indomethacin, were weak inhibitors of the enzymes. On the other hand, meclofenamic acid was a competitive inhibitor of the enzymes with an apparent Ki of 3.0 x 10-4 M. Possible significance of these findings in arachidonic acid metabolism is discussed.en_US
dc.format.extent361229 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleIndomethacin inhibition of glutathione S-transferasesen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelNatural Resources and Environmenten_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelEcology and Evolutionary Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry The University of Michigan Medical School, Ann Arbor, Michigan 48109, U.S.A.; The Montgomery Allergy Research Laboratory, Department of Internal Medicine, The University of Michigan Medical School, Ann Arbor, Michigan 48109, U.S.A.en_US
dc.contributor.affiliationumDepartment of Biological Chemistry The University of Michigan Medical School, Ann Arbor, Michigan 48109, U.S.A.; The Montgomery Allergy Research Laboratory, Department of Internal Medicine, The University of Michigan Medical School, Ann Arbor, Michigan 48109, U.S.A.en_US
dc.identifier.pmid6847692en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/25218/1/0000658.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0006-291X(83)91714-Xen_US
dc.identifier.sourceBiochemical and Biophysical Research Communicationsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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