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IMMUNOHISTOCHEMICAL LOCALIZATION AND ACTIVITY OF GLUTATHIONE TRANSFERASE ZETA (GSTZ1-1) IN RAT TISSUES

dc.contributor.authorLantum, Hoffman
dc.contributor.authorBaggs, Raymond
dc.contributor.authorKrenitsky, Daria
dc.contributor.authorBoard, Philip
dc.contributor.authorAnders, Michael
dc.date.accessioned2015-12-13T23:21:10Z
dc.date.issued2002
dc.date.updated2015-12-12T09:05:48Z
dc.description.abstractGlutathione transferase zeta (GSTZ1-1) catalyzes the biotransformation of a range of α-haloacids, including dichloroacetic acid (DCA), and the penultimate step in the tyrosine degradation pathway. DCA is a rodent carcinogen and a common drinking water co
dc.identifier.issn0090-9556
dc.identifier.urihttp://hdl.handle.net/1885/91063
dc.publisherAmerican Society for Pharmacology and Experimental Therapeutics
dc.sourceDrug Metabolism and Disposition
dc.subjectKeywords: acetic acid; acetone; alpha haloacid derivative; carcinogen; chlorofluoroacetic acid; dichloroacetic acid; drinking water; glutathione transferase; glutathione transferase zeta; haloacid; maleylacetone; tyrosine; unclassified drug; adrenal medulla; airway
dc.titleIMMUNOHISTOCHEMICAL LOCALIZATION AND ACTIVITY OF GLUTATHIONE TRANSFERASE ZETA (GSTZ1-1) IN RAT TISSUES
dc.typeJournal article
local.bibliographicCitation.issue6
local.bibliographicCitation.lastpage625
local.bibliographicCitation.startpage616
local.contributor.affiliationLantum, Hoffman, University of Rochester
local.contributor.affiliationBaggs, Raymond, University of Rochester
local.contributor.affiliationKrenitsky, Daria, University of Rochester
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.ariespublicationMigratedxPub21695
local.identifier.citationvolume30
local.identifier.doi10.1124/dmd.30.6.616
local.identifier.scopusID2-s2.0-0036265997
local.type.statusPublished Version

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