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Glutathione transferase zeta-catalyzed biotransformation of deuterated dihaloacetic acids

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dc.contributor.authorWerkmeister, Jerome A
dc.contributor.authorAnderson, Warwick P
dc.contributor.authorTzeng, Huey-Fen
dc.contributor.authorBoard, Philip
dc.contributor.authorAnders, Michael
dc.date.accessioned2015-12-13T23:25:08Z
dc.date.issued1999
dc.date.updated2015-12-12T09:23:40Z
dc.description.abstractGlutathione transferase zeta (GSTZ) catalyzes the biotransformation of α-haloalkanoic acids. Treatment of rats or humans with dichloroacetic acid prolongs its elimination half-life, and preliminary studies in this laboratory show that fluorine-lacking, b
dc.identifier.issn0006-291X
dc.identifier.urihttp://hdl.handle.net/1885/92532
dc.publisherAcademic Press
dc.sourceBiochemical and Biophysical Research Communications
dc.subjectKeywords: acetic acid derivative; deuterium; dichloroacetic acid; fluorine; glutathione transferase; glyoxylic acid; haloacid; isoenzyme; article; biotransformation; catalysis; half life time; human; nonhuman; priority journal; rat; Acetic Acids; Animals; Biotransf
dc.titleGlutathione transferase zeta-catalyzed biotransformation of deuterated dihaloacetic acids
dc.typeJournal article
local.bibliographicCitation.issue3
local.bibliographicCitation.lastpage783
local.bibliographicCitation.startpage779
local.contributor.affiliationWerkmeister, Jerome A, CSIRO Molecular and Health Technologies
local.contributor.affiliationAnderson, Warwick P, Monash University
local.contributor.affiliationTzeng, Huey-Fen, National Chi Nan University
local.contributor.affiliationBoard, Philip, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationAnders, Michael, University of Rochester
local.contributor.authoruidBoard, Philip, u7701651
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.absfor060107 - Enzymes
local.identifier.ariespublicationMigratedxPub23651
local.identifier.citationvolume261
local.identifier.doi10.1006/bbrc.1999.1127
local.identifier.scopusID2-s2.0-0033546719
local.type.statusPublished Version

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