The impact of heavy metals on the activity of carbonic anhydrase from rainbow trout (Oncorhynchus mykiss) kidney

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dc.authorid23502381000
dc.authorid6603903192
dc.contributor.authorSöyüt H.
dc.contributor.authorBeydemir S.
dc.date.accessioned20.04.201910:49:12
dc.date.accessioned2019-04-20T21:44:39Z
dc.date.available20.04.201910:49:12
dc.date.available2019-04-20T21:44:39Z
dc.date.issued2012
dc.departmentBayburt Üniversitesien_US
dc.description.abstractMany environmental and health problems have become a consequence of contamination of soil and water by toxic heavy metals and organic pollutants in the present age of technology. Heavy metals play vital roles in enzyme activities and other metabolic events with their bioaccumulative and nonbiodegradable properties among aquatic pollutants. Metal toxicity causes irregular metallothioneins protein synthesis, renal damage, and disruption of bone structure in humans and wildlife. In this study, we investigated in vitro effects of some metals on chemical-targeted carbonic anhydrase (CA) enzyme from rainbow trout kidney. The enzyme was purified with a specific activity of 17,285 EU × mg-1 and 31.7% yield and approximately 1800-fold using simple affinity purification method. Molecular weights of the subunit and native enzyme were estimated as 28.7 kDa and 26.9 kDa via sodium dodecyl sulfate polyacrylamide gel electrophoresis and Sephadex-G 200 column, respectively. Other kinetic properties of the enzyme were determined. Apparent Km, Vmax and kcat values were 0.40 mM, 0.097 ?mol min-1 and 15.2 s-1 for p-nitrophenylacetate substrate, respectively. Inhibitory effects of cobalt, zinc, copper, cadmium and silver on CA activity were determined using the esterase method under in vitro conditions. IC50 and Ki values were calculated for metals. Ki values for Co2+, Zn2+, Cu2+, Cd2+ and Ag+ were 0.035, 1.2, 34.8, 103 and 257 from Lineweaver-Burk graphs, respectively. Consequently, in vitro inhibition rank order was determined as Co2+ > Zn2+ > Cu 2+ > Cd2+ > Ag+. The potential inhibitor for CA was found as Co2+ from these results. © 2011 The Author(s).en_US
dc.identifier.doi10.1177/0748233711410914
dc.identifier.endpage305
dc.identifier.issn0748-2337
dc.identifier.issue4
dc.identifier.pmid21949088en_US
dc.identifier.scopus2-s2.0-84861833727en_US
dc.identifier.scopusqualityQ3en_US
dc.identifier.startpage296
dc.identifier.urihttps://dx.doi.org/10.1177/0748233711410914
dc.identifier.urihttps://hdl.handle.net/20.500.12403/903
dc.identifier.volume28
dc.identifier.wosWOS:000302628600002en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.relation.ispartofToxicology and Industrial Healthen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectCarbonic anhydrase
dc.subjectinhibition
dc.subjectkidney
dc.subjectmetal toxicity
dc.subjectrainbow trout
dc.subject4 nitrophenylacetic acid
dc.subjectcadmium
dc.subjectcarbonate dehydratase
dc.subjectcobalt
dc.subjectcopper
dc.subjectesterase
dc.subjectheavy metal
dc.subjectmetallothionein
dc.subjectphenylacetic acid
dc.subjectsephadex
dc.subjectsilver
dc.subjectunclassified drug
dc.subjectzinc
dc.subjectarticle
dc.subjectbinding affinity
dc.subjectbone structure
dc.subjectcontrolled study
dc.subjectenzyme activity
dc.subjectenzyme assay
dc.subjectenzyme kinetics
dc.subjectenzyme purification
dc.subjectIC 50
dc.subjectkidney
dc.subjectkidney injury
dc.subjectmetal toxicity
dc.subjectmolecular weight
dc.subjectnonhuman
dc.subjectpolyacrylamide gel electrophoresis
dc.subjectprotein purification
dc.subjectprotein synthesis
dc.subjectrainbow trout
dc.subjectAnimals
dc.subjectCarbonic Anhydrase Inhibitors
dc.subjectCarbonic Anhydrases
dc.subjectHydrogen-Ion Concentration
dc.subjectInhibitory Concentration 50
dc.subjectKidney
dc.subjectKinetics
dc.subjectLinear Models
dc.subjectMetals, Heavy
dc.subjectOncorhynchus mykiss
dc.subjectOncorhynchus mykiss
dc.subjectCarbonic anhydrase
dc.subjectinhibition
dc.subjectkidney
dc.subjectmetal toxicity
dc.subjectrainbow trout
dc.subject4 nitrophenylacetic acid
dc.subjectcadmium
dc.subjectcarbonate dehydratase
dc.subjectcobalt
dc.subjectcopper
dc.subjectesterase
dc.subjectheavy metal
dc.subjectmetallothionein
dc.subjectphenylacetic acid
dc.subjectsephadex
dc.subjectsilver
dc.subjectunclassified drug
dc.subjectzinc
dc.subjectarticle
dc.subjectbinding affinity
dc.subjectbone structure
dc.subjectcontrolled study
dc.subjectenzyme activity
dc.subjectenzyme assay
dc.subjectenzyme kinetics
dc.subjectenzyme purification
dc.subjectIC 50
dc.subjectkidney
dc.subjectkidney injury
dc.subjectmetal toxicity
dc.subjectmolecular weight
dc.subjectnonhuman
dc.subjectpolyacrylamide gel electrophoresis
dc.subjectprotein purification
dc.subjectprotein synthesis
dc.subjectrainbow trout
dc.subjectAnimals
dc.subjectCarbonic Anhydrase Inhibitors
dc.subjectCarbonic Anhydrases
dc.subjectHydrogen-Ion Concentration
dc.subjectInhibitory Concentration 50
dc.subjectKidney
dc.subjectKinetics
dc.subjectLinear Models
dc.subjectMetals, Heavy
dc.subjectOncorhynchus mykiss
dc.subjectOncorhynchus mykiss
dc.titleThe impact of heavy metals on the activity of carbonic anhydrase from rainbow trout (Oncorhynchus mykiss) kidneyen_US
dc.typeArticleen_US

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