Please use this identifier to cite or link to this item: https://hdl.handle.net/11499/4117
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dc.contributor.authorŞen, Alaattin.-
dc.contributor.authorSemiz, Aslı.-
dc.date.accessioned2019-08-16T11:32:18Z
dc.date.available2019-08-16T11:32:18Z
dc.date.issued2007-
dc.identifier.issn0147-6513-
dc.identifier.urihttps://hdl.handle.net/11499/4117-
dc.identifier.urihttps://doi.org/10.1016/j.ecoenv.2006.08.007-
dc.description.abstractIn this study, feral leaping mullet (Liza saliens) liver microsomal 7-ethoxyresorufin O-deethylase (EROD), and cytosolic glutathione S-transferases (GSTs) activities were investigated using 7-ethoxyresorufin, 1-chloro-2,4-dinitrobenzene (CDNB), and ethacrynic acid (EA) as substrates, respectively. The average EROD activity was found as 1139±175 pmol resorufin/min/mg protein. The average GST activities towards CDNB and EA were found as 1364±41 and 140±19 nmol/min/mg protein, respectively. We have, then, investigated the in vitro effects of some metals and detergents on CYP1A and GST activities in leaping mullet liver. Leaping mullet liver microsomal EROD activity was significantly inhibited by Hg (0.1 mM), Ni (0.1 mM), Cd (0.1 mM), Cu (0.1 mM), Zn (0.1 mM), Sb (0.1 mM), Fe2+ (1 mM), Co (1 mM), Al (1 mM), and Fe3+ (1 mM), with the percent inhibition of 80, 80, 77, 75, 70, 69, 56, 53, 46, and 44, respectively. Similarly, conjugation of CDNB catalyzed by GST was inhibited significantly to lesser extend by Hg (0.1 mM), Sb (0.1 mM), Cd (0.1 mM), Cu (0.1 mM), Zn (0.1 mM), Fe3+ (1 mM), Co (1 mM), and Fe2+ (1 mM), with the percent inhibition of 70, 69, 65, 61, 54, 51, 47, and 43, respectively. The degrees of inhibition observed on GST catalyzed EA conjugation by Hg (0.1 mM), Cd (0.1 mM), Sb (0.1 mM), Cu (0.1 mM), and Zn (0.1 mM) were 86, 78, 69, 51, and 42, respectively. In addition to metals, the effect of various detergents on leaping mullet liver EROD, GST-CDNB, and GST-EA activities were studied. It was found that ionic detergents strongly inhibited the EROD activity, whereas much less inhibitions were observed with GST catalyzed activities. Therefore, the CYP1A inhibition potencies of metals and detergents suggest that their contribution to the overall CYP1A induction in polycyclic aromatic hydrocarbons contaminated environmental samples has to be taken into account for better interpretation of environmental studies. © 2006 Elsevier Inc. All rights reserved.en_US
dc.language.isoenen_US
dc.relation.ispartofEcotoxicology and Environmental Safetyen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subject7-Ethoxyresorufin O-deethylaseen_US
dc.subjectBiomarkersen_US
dc.subjectDetergentsen_US
dc.subjectGlutathione S-transferasesen_US
dc.subjectInhibitionen_US
dc.subjectLiza saliensen_US
dc.subjectMetalsen_US
dc.subjectMulleten_US
dc.subject1 chloro 2,4 dinitrobenzeneen_US
dc.subjectaluminumen_US
dc.subjectantimonyen_US
dc.subjectcadmiumen_US
dc.subjectcobalten_US
dc.subjectcopperen_US
dc.subjectcytochrome P450 1Aen_US
dc.subjectdetergenten_US
dc.subjectetacrynic aciden_US
dc.subjectethoxyresorufinen_US
dc.subjectethoxyresorufin deethylaseen_US
dc.subjectferrous ionen_US
dc.subjectglutathioneen_US
dc.subjectglutathione transferaseen_US
dc.subjectmicrosome enzymeen_US
dc.subjectnickelen_US
dc.subjectzincen_US
dc.subjectbiomarkeren_US
dc.subjectbiotransformationen_US
dc.subjectenzyme activityen_US
dc.subjectmetalen_US
dc.subjectPAHen_US
dc.subjectperciformen_US
dc.subjectpollution effecten_US
dc.subjectaquatic environmenten_US
dc.subjectaquatic speciesen_US
dc.subjectarticleen_US
dc.subjectconjugationen_US
dc.subjectcontrolled studyen_US
dc.subjectdetoxificationen_US
dc.subjectenzyme inhibitionen_US
dc.subjectenzyme substrateen_US
dc.subjectin vitro studyen_US
dc.subjectliveren_US
dc.subjectliver microsomeen_US
dc.subjectnonhumanen_US
dc.subjectstatistical significanceen_US
dc.subjectAnimalsen_US
dc.subjectBiological Markersen_US
dc.subjectBiotransformationen_US
dc.subjectCytochrome P-450 CYP1A1en_US
dc.subjectDinitrochlorobenzeneen_US
dc.subjectEnvironmental Monitoringen_US
dc.subjectEnzyme Inhibitorsen_US
dc.subjectEthacrynic Aciden_US
dc.subjectFish Proteinsen_US
dc.subjectGlutathione Transferaseen_US
dc.subjectLiveren_US
dc.subjectMetabolic Detoxication, Drugen_US
dc.subjectMicrosomes, Liveren_US
dc.subjectOxazinesen_US
dc.subjectSmegmamorphaen_US
dc.subjectSubstrate Specificityen_US
dc.subjectWater Pollutants, Chemicalen_US
dc.titleEffects of metals and detergents on biotransformation and detoxification enzymes of leaping mullet (Liza saliens)en_US
dc.typeArticleen_US
dc.identifier.volume68en_US
dc.identifier.issue3en_US
dc.identifier.startpage405
dc.identifier.startpage405en_US
dc.identifier.endpage411en_US
dc.identifier.doi10.1016/j.ecoenv.2006.08.007-
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.pmid17011620en_US
dc.identifier.scopus2-s2.0-34848832885en_US
dc.identifier.wosWOS:000251067500011en_US
dc.identifier.scopusqualityQ1-
dc.ownerPamukkale University-
item.grantfulltextnone-
item.openairetypeArticle-
item.cerifentitytypePublications-
item.fulltextNo Fulltext-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
crisitem.author.dept17.02. Biology-
crisitem.author.dept20.03. Biomedical Engineering-
Appears in Collections:Fen-Edebiyat Fakültesi Koleksiyonu
PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
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