Characterization of aldrin epoxidation in flathead mullet (Mugil cephalus) liver microsomes: Involvement of CYP3A

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dc.authorid0000-0002-6949-9191
dc.authorid0000-0002-8754-2528
dc.authorid0000-0002-0107-0110
dc.contributor.authorBozcaarmutlu, Azra
dc.contributor.authorTurna, Sema
dc.contributor.authorErden, Canan Sapmaz
dc.contributor.authorYenisoy-Karakaş, Serpil
dc.contributor.authorArınç, E.
dc.date.accessioned2021-06-23T19:27:47Z
dc.date.available2021-06-23T19:27:47Z
dc.date.issued2011
dc.departmentBAİBÜ, Fen Edebiyat Fakültesi, Kimya Bölümüen_US
dc.description47th Congress of the European-Societies-of-Toxicology -- AUG 28-31, 2011 -- Paris, FRANCEen_US
dc.description.abstractToxic organochlorine pesticides, aldrin and its metabolite dieldrin, have been reported to contaminate the aquatic environment highly. In the present study, epoxidation reaction of aldrin to dieldrin was studied in mullet liver microsomes and contribution of cytochrome P450 isozyme(s) was determined by using specific cytochrome P450 inhibitors and substrate. Flathead mullet samples (Mugil cephalus) were caught from the West Black Sea Region of Turkey. Fish liver microsomes were prepared by differential centrifugation. Epoxidation of aldrin to dieldrin was determined by measuring the amount of dieldrin produced using gas chromatography and electron capture detector. Aldrin epoxidation was linear with time up to 60 min and with protein concentration up to 10 mg/mL. Maximal fish liver aldrin epoxidase activity was observed at pH 7.6. Aldrin epoxidase exhibited monophasic kinetics with apparent Km value of 140 μM for aldrin. The enzyme activity was inhibited approximately by 9% and 16% by methanol and DMSO, respectively. On the other hand, aldrin epoxidation was enhanced by about 113% with 2% ethanol in the incubation medium. Ketoconazole (CYP3A inhibitor), potentially inhibited the metabolism of aldrin, tolbutamide (CYP2C substrate), and alpha-naphthoflavone (CYP1A inhibitor) did not show inhibition. The results of this study strongly suggest that CYP3A is the cytochrome P450 isozyme involved in aldrin epoxidation in mullet liver microsomes whereas CYP2C and CYP1A are not involved.en_US
dc.description.sponsorshipEuropean Soc Toxicolen_US
dc.identifier.doi10.1016/j.toxlet.2011.05.650
dc.identifier.endpageS187en_US
dc.identifier.issn0378-4274
dc.identifier.startpageS187en_US
dc.identifier.urihttps://doi.org/10.1016/j.toxlet.2011.05.650
dc.identifier.urihttps://hdl.handle.net/20.500.12491/6891
dc.identifier.volume205en_US
dc.identifier.wosWOS:000293814500598en_US
dc.identifier.wosqualityQ1en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.institutionauthorBozcaarmutlu, Azra
dc.language.isoenen_US
dc.publisherElsevier Ireland Ltden_US
dc.relation.ispartofToxicology Lettersen_US
dc.relation.publicationcategoryKonferans Öğesi - Uluslararası - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectMugil Cephalusen_US
dc.titleCharacterization of aldrin epoxidation in flathead mullet (Mugil cephalus) liver microsomes: Involvement of CYP3Aen_US
dc.typeConference Objecten_US

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