Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/13462
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dc.contributor.authorBaldwin, Graham Sen
dc.contributor.authorAbbott, F Sen
dc.contributor.authorNau, Hen
dc.date.accessioned2015-05-16T03:18:59Z
dc.date.available2015-05-16T03:18:59Z
dc.date.issued1996-04-08en
dc.identifier.citationFebs Letters; 384(1): 58-60en
dc.identifier.govdoc8797803en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/13462en
dc.description.abstractThe anti-convulsant drug valproate causes hepatic failure in a small percentage of patients. We now report that the valproate metabolite 2,4-dien-valproate binds (IC50 = 42 microM) to the alpha-subunit of the trifunctional protein responsible for the second and third steps in the mitochondrial beta-oxidation of fatty acids. Binding of valproate itself, or of the metabolites 2-envalproate, 4-en-valproate or 3-hydroxy-4-en-valproate, is considerably weaker. We conclude that valproate-induced hepatotoxicity may be due in part to the reversible binding of the valproate metabolite 2,4-dien-valproate or its CoA ester to the alpha-subunit of the trifunctional protein with consequent inhibition of fatty acid oxidation.en
dc.language.isoenen
dc.subject.otherAnimalsen
dc.subject.otherAnticonvulsants.metabolism.toxicityen
dc.subject.otherFatty Acids.metabolismen
dc.subject.otherGastric Mucosa.metabolismen
dc.subject.otherKineticsen
dc.subject.otherLiver.drug effects.pathologyen
dc.subject.otherMacromolecular Substancesen
dc.subject.otherMitochondrial Trifunctional Proteinen
dc.subject.otherMultienzyme Complexes.isolation & purification.metabolismen
dc.subject.otherOxidation-Reductionen
dc.subject.otherProtein Bindingen
dc.subject.otherSwineen
dc.subject.otherValproic Acid.analogs & derivatives.metabolism.toxicityen
dc.titleBinding of a valproate metabolite to the trifunctional protein of fatty acid oxidation.en
dc.typeJournal Articleen
dc.identifier.journaltitleFEBS lettersen
dc.identifier.affiliationDepartment of Surgery, Austin Hospital, Heidelberg, Victoria, Australiaen
dc.description.pages58-60en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/8797803en
dc.type.austinJournal Articleen
item.grantfulltextnone-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeJournal Article-
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
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