Carbonic anhydrase activity from the gilthead sea bream (Sparus aurata) liver: The toxicological effects of heavy metals

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dc.authorid55537752500
dc.authorid23502381000
dc.authorid6603903192
dc.contributor.authorKaya E.D.
dc.contributor.authorSöyüt H.
dc.contributor.authorBeydemir T.
dc.date.accessioned20.04.201910:49:12
dc.date.accessioned2019-04-20T21:44:24Z
dc.date.available20.04.201910:49:12
dc.date.available2019-04-20T21:44:24Z
dc.date.issued2013
dc.departmentBayburt Üniversitesien_US
dc.description.abstractMany studies have shown that metal ions may lead to oxidative stress in biological systems. Accordingly, DNA damage, protein modification, enzyme inhibition and activation, lipid peroxidation and many other effects may occur in living organisms. Many different formations of metal ions may enter human cells along with water, air, and various foods, and humans are negatively affected by these conditions, either directly or indirectly. These effects may cause irreversible damage to human metabolism. In this study, the toxicological effects of heavy metals on carbonic anhydrase enzyme activity from the gilthead sea bream liver were investigated. The carbonic anhydrase enzyme was purified via affinity chromatography and had a specific activity of 6775.5EUmg-1. The kinetics and characteristic properties, such as optimum pH, stable pH, optimum temperature, activation energy (Ea), activation enthalpy (?H), Q10, Km, and Vmax, were determined for the purified enzyme SDS-polyacrylamide gel electrophoresis showed a single band and molecular weight of the subunit was approximately 25kDa. Cd(II), Cu(II), Ni(II) and Ag(I) inhibited the enzyme activity in vitro. The type of inhibition and Ki values for these metals were calculated from Lineweaver-Burk plots as 17.74mM, 36.20mM, 12.85mM and 0.025mM for Cd(II), Cu(II), Ni(II) and Ag(I), respectively. All the metals were noncompetitive inhibitors. © 2013 The Authors.en_US
dc.identifier.doi10.1016/j.etap.2013.05.019
dc.identifier.endpage521
dc.identifier.issn1382-6689
dc.identifier.issue2
dc.identifier.pmid23811108en_US
dc.identifier.scopus2-s2.0-84879768228en_US
dc.identifier.scopusqualityN/Aen_US
dc.identifier.startpage514
dc.identifier.urihttps://dx.doi.org/10.1016/j.etap.2013.05.019
dc.identifier.urihttps://hdl.handle.net/20.500.12403/849
dc.identifier.volume36
dc.identifier.wosWOS:000324082900031en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.relation.ispartofEnvironmental Toxicology and Pharmacologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectCarbonic anhydrase
dc.subjectFish
dc.subjectHeavy metals
dc.subjectInhibition
dc.subjectLiver
dc.subjectcadmium
dc.subjectcarbonate dehydratase
dc.subjectcopper
dc.subjectheavy metal
dc.subjectnickel
dc.subjectsilver
dc.subjectaffinity chromatography
dc.subjectanimal tissue
dc.subjectarticle
dc.subjectcontrolled study
dc.subjectenergy
dc.subjectenthalpy
dc.subjectenzyme activity
dc.subjectenzyme analysis
dc.subjectenzyme kinetics
dc.subjectenzyme purification
dc.subjectenzyme stability
dc.subjectheavy metal poisoning
dc.subjectin vitro study
dc.subjectliver
dc.subjectmolecular weight
dc.subjectnonhuman
dc.subjectoxidative stress
dc.subjectpH measurement
dc.subjectpollution
dc.subjectpolyacrylamide gel electrophoresis
dc.subjectpriority journal
dc.subjectSparus aurata
dc.subjecttemperature measurement
dc.subjectCA
dc.subjectcarbonic anhydrase
dc.subjectCarbonic anhydrase
dc.subjectFish
dc.subjectHeavy metals
dc.subjectInhibition
dc.subjectLiver
dc.subjectmolecular weight
dc.subjectMW
dc.subjectrainbow trout
dc.subjectRT
dc.subjectSDS-PAGE
dc.subjectsodium dodecyl sulfate polyacrylamide gel electrophoresis
dc.subjectAnimals
dc.subjectCarbonic Anhydrase Inhibitors
dc.subjectCarbonic Anhydrases
dc.subjectChromatography, Affinity
dc.subjectDose-Response Relationship, Drug
dc.subjectFish Proteins
dc.subjectKinetics
dc.subjectLiver
dc.subjectMetals, Heavy
dc.subjectModels, Biological
dc.subjectSea Bream
dc.subjectWater Pollutants, Chemical
dc.subjectArchosargus rhomboidalis
dc.subjectSparus aurata
dc.subjectCarbonic anhydrase
dc.subjectFish
dc.subjectHeavy metals
dc.subjectInhibition
dc.subjectLiver
dc.subjectcadmium
dc.subjectcarbonate dehydratase
dc.subjectcopper
dc.subjectheavy metal
dc.subjectnickel
dc.subjectsilver
dc.subjectaffinity chromatography
dc.subjectanimal tissue
dc.subjectarticle
dc.subjectcontrolled study
dc.subjectenergy
dc.subjectenthalpy
dc.subjectenzyme activity
dc.subjectenzyme analysis
dc.subjectenzyme kinetics
dc.subjectenzyme purification
dc.subjectenzyme stability
dc.subjectheavy metal poisoning
dc.subjectin vitro study
dc.subjectliver
dc.subjectmolecular weight
dc.subjectnonhuman
dc.subjectoxidative stress
dc.subjectpH measurement
dc.subjectpollution
dc.subjectpolyacrylamide gel electrophoresis
dc.subjectpriority journal
dc.subjectSparus aurata
dc.subjecttemperature measurement
dc.subjectCA
dc.subjectcarbonic anhydrase
dc.subjectCarbonic anhydrase
dc.subjectFish
dc.subjectHeavy metals
dc.subjectInhibition
dc.subjectLiver
dc.subjectmolecular weight
dc.subjectMW
dc.subjectrainbow trout
dc.subjectRT
dc.subjectSDS-PAGE
dc.subjectsodium dodecyl sulfate polyacrylamide gel electrophoresis
dc.subjectAnimals
dc.subjectCarbonic Anhydrase Inhibitors
dc.subjectCarbonic Anhydrases
dc.subjectChromatography, Affinity
dc.subjectDose-Response Relationship, Drug
dc.subjectFish Proteins
dc.subjectKinetics
dc.subjectLiver
dc.subjectMetals, Heavy
dc.subjectModels, Biological
dc.subjectSea Bream
dc.subjectWater Pollutants, Chemical
dc.subjectArchosargus rhomboidalis
dc.subjectSparus aurata
dc.titleCarbonic anhydrase activity from the gilthead sea bream (Sparus aurata) liver: The toxicological effects of heavy metalsen_US
dc.typeArticleen_US

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