Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/9374
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dc.contributor.authorChing, M Sen
dc.contributor.authorBlake, C Len
dc.contributor.authorMalek, N Aen
dc.contributor.authorAngus, Peter Wen
dc.contributor.authorGhabrial, Hanyen
dc.date.accessioned2015-05-15T22:26:49Z
dc.date.available2015-05-15T22:26:49Z
dc.date.issued2001-11-01en
dc.identifier.citationXenobiotica; the Fate of Foreign Compounds in Biological Systems; 31(11): 757-67en
dc.identifier.govdoc11765139en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/9374en
dc.description.abstract1. The inhibition of recombinant CYP1A1 and CYP1A2 activity by quinidine and quinine was evluated using ethoxyresorutin O-deethylation, phenacetin O-deethylation and propranolol desisopropylation as probe catalytic pathways. 2. With substrate concentrations near the Km of catalysis, both quinidine and quinine potently inhibited CYP1A1 activity with [I](0.5) approximately 1-3 microM, whereas in contrast, there was little inhibition of CYP1A2 activity. The Lineweaver-Burk plots with varying inhibitor concentrations suggested that inhibition by quinidine and quinine was competitive. 3. There was only trace metabolism of quinidine by recombinant CYP1A1, whereas rat liver microsomes as a control showed extensive consumption of quinidine and metabolite production. 4. This work suggests that quinidine is a non-classical inhibitor of CYP1A1 and that it is not as highly specific at inhibiting CYP2D6 as previously thought.en
dc.language.isoenen
dc.subject.otherAcetaminophen.metabolismen
dc.subject.otherAnimalsen
dc.subject.otherCytochrome P-450 CYP1A1.antagonists & inhibitors.genetics.metabolismen
dc.subject.otherCytochrome P-450 CYP1A2.genetics.metabolismen
dc.subject.otherCytochrome P-450 CYP1A2 Inhibitorsen
dc.subject.otherEnzyme Inhibitors.pharmacologyen
dc.subject.otherHumansen
dc.subject.otherMicrosomes, Liver.drug effects.metabolismen
dc.subject.otherOxazines.metabolismen
dc.subject.otherPhenacetin.metabolism.pharmacologyen
dc.subject.otherQuinidine.pharmacologyen
dc.subject.otherQuinine.pharmacologyen
dc.subject.otherRatsen
dc.subject.otherRecombinant Proteins.antagonists & inhibitors.genetics.metabolismen
dc.subject.otherYeasts.geneticsen
dc.titleDifferential inhibition of human CYP1A1 and CYP1A2 by quinidine and quinine.en
dc.typeJournal Articleen
dc.identifier.journaltitleXenobiotica; the fate of foreign compounds in biological systemsen
dc.identifier.affiliationDepartment of Medicine, University of Melbourne, Austin & Repatriation Medical Centre, Victoria, Australiaen
dc.identifier.doi10.1080/00498250110065603en
dc.description.pages757-67en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/11765139en
dc.type.austinJournal Articleen
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeJournal Article-
item.grantfulltextnone-
item.cerifentitytypePublications-
item.fulltextNo Fulltext-
crisitem.author.deptVictorian Liver Transplant Unit-
crisitem.author.deptGastroenterology and Hepatology-
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