Glutathione transferase zeta: novel xenobiotic substrates and enzyme inactivation

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dc.contributor.authorAnders, Michael
dc.contributor.authorAnderson, Wayne
dc.contributor.authorTzeng, Huey-Fen
dc.contributor.authorBoard, Philip
dc.date.accessioned2015-12-13T23:16:30Z
dc.date.available2015-12-13T23:16:30Z
dc.date.issued2001
dc.date.updated2015-12-12T08:48:26Z
dc.description.abstractGlutathione transferase zeta (GSTZ1-1) catalyzes the biotransformation of a range of α-haloalkanoates and the isomerization of maleylacetoacetate to furmarylacetoacetate. The elimination half-life of DCA is increased in human subjects or rats given singl
dc.identifier.issn0009-2797
dc.identifier.urihttp://hdl.handle.net/1885/89443
dc.publisherElsevier
dc.sourceChemico-Biological Interactions
dc.subjectKeywords: Dichloroacetate; Enzyme inactivation; Glutathione transferase zeta; Maleylacetoacetate isomerase
dc.titleGlutathione transferase zeta: novel xenobiotic substrates and enzyme inactivation
dc.typeJournal article
local.bibliographicCitation.lastpage216
local.bibliographicCitation.startpage211
local.contributor.affiliationAnders, Michael, University of Rochester
local.contributor.affiliationAnderson, Wayne, University of Rochester Medical Center
local.contributor.affiliationTzeng, Huey-Fen, National Chi Nan University
local.contributor.affiliationBoard, Philip, College of Medicine, Biology and Environment, ANU
local.contributor.authoruidBoard, Philip, u7701651
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.absfor060107 - Enzymes
local.identifier.ariespublicationMigratedxPub19472
local.identifier.citationvolume133
local.identifier.scopusID2-s2.0-0003198476
local.type.statusPublished Version

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