Effects of some metal ions on trout liver glucose 6-phosphate Dehydrogenase

ArticleAçık Erişim

Özet

Information on the mechanism of metal ion inhibition of Glucose 6-phosphate dehydrogenase (G6PD) is limited. The purpose of the present study was to clarify in vitro effect of Hg +2, Cd +2, Pb +2, Fe +2, Cu +2 and Zn +2ions on the purified glucose 6-phosphate dehydrogenase (G6PD). This enzyme was purified from rainbow trout liver (Oncorhynchus mykiss) by 2',5'-ADP sepharose 4B affinity gel chromatography. G6PD was purified 1010-fold with a yield of 41.72%. Purity of enzyme checked by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) method and a single band was observed. All of the metal ions caused inhibition of the enzyme activity. Of the metal ions tested, Fe +2 exhibited much higher inhibitory effect at lower concentrations, so it was evidently a more potent inhibitor than the others. Hg +2, Cd +2, Pb +2, Cu +2 and Zn +2 displayed noncompetitive type of inhibition mechanism only Fe +2 exhibited competitive type inhibition. IC 50 value of Fe +2, Pb +2, Hg +2, Cu +2, Zn +2 and Cd +2 were 0.39, 0.78, 0.87, 1.19, 1.97, 2.16 and the Ki constants 0.197±0.049, 0.213±0.018, 0.542±0.029, 1.721±0.77, 2.034±0.53 and 2.770±1.21, respectively. © 2011 Academic Journals Inc.

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RDL Kalıcı Bağlantı (PID)
https://rdlopen.rawdatalibrary.net/r/ebyu/15925Resmi atıflarda kullanılan kalıcı adres
DOI
https://doi.org/10.3923/rjet.2011.385.391Yayıncı resmi DOI adresi
Tam Kayıt
AlanDeğerDil
dc.contributor.authorCankaya, M.
dc.contributor.authorSisecioglu, M.
dc.contributor.authorCiftci, M.
dc.contributor.authorOzdemir, H.
dc.date.accessioned2026-10-18T20:30:46.331077056Z
dc.date.available2026-10-18T20:30:46.331077056Z
dc.date.issued2011
dc.description.abstractInformation on the mechanism of metal ion inhibition of Glucose 6-phosphate dehydrogenase (G6PD) is limited. The purpose of the present study was to clarify in vitro effect of Hg +2, Cd +2, Pb +2, Fe +2, Cu +2 and Zn +2ions on the purified glucose 6-phosphate dehydrogenase (G6PD). This enzyme was purified from rainbow trout liver (Oncorhynchus mykiss) by 2',5'-ADP sepharose 4B affinity gel chromatography. G6PD was purified 1010-fold with a yield of 41.72%. Purity of enzyme checked by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) method and a single band was observed. All of the metal ions caused inhibition of the enzyme activity. Of the metal ions tested, Fe +2 exhibited much higher inhibitory effect at lower concentrations, so it was evidently a more potent inhibitor than the others. Hg +2, Cd +2, Pb +2, Cu +2 and Zn +2 displayed noncompetitive type of inhibition mechanism only Fe +2 exhibited competitive type inhibition. IC 50 value of Fe +2, Pb +2, Hg +2, Cu +2, Zn +2 and Cd +2 were 0.39, 0.78, 0.87, 1.19, 1.97, 2.16 and the Ki constants 0.197±0.049, 0.213±0.018, 0.542±0.029, 1.721±0.77, 2.034±0.53 and 2.770±1.21, respectively. © 2011 Academic Journals Inc.
dc.identifier.doi10.3923/rjet.2011.385.391
dc.identifier.endpage391
dc.identifier.issn1819-3420
dc.identifier.issue6
dc.identifier.scopus2-s2.0-84857151698
dc.identifier.startpage385
dc.identifier.urihttps://rdlopen.rawdatalibrary.net/r/ebyu/15925
dc.identifier.volume5
dc.language.isoen
dc.relation.ispartofResearch Journal of Environmental Toxicology
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectG6PD enzyme
dc.subjectInhibition
dc.subjectMetal ions
dc.subjectcadmium
dc.subjectcopper
dc.subjectglucose 6 phosphatase
dc.subjectiron
dc.subjectlead
dc.subjectmercury
dc.subjectzinc
dc.subjectaffinity chromatography
dc.subjectanimal tissue
dc.subjectarticle
dc.subjectcompetitive inhibition
dc.subjectconcentration (parameters)
dc.subjectcontrolled study
dc.subjectenzyme activity
dc.subjectenzyme inhibition
dc.subjectgel chromatography
dc.subjectin vitro study
dc.subjectnonhuman
dc.subjectpolyacrylamide gel electrophoresis
dc.subjectrainbow trout
dc.titleEffects of some metal ions on trout liver glucose 6-phosphate Dehydrogenase
dc.typeArticle
dspace.entity.typePublication
rdl.citation.scopus15
rdl.oa.statusopen
rdl.source.indexSCOPUS