Purification and characterization of glutathione-S-transferase from chicken erythrocyte

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dc.contributor.authorAydemir T.
dc.contributor.authorKavrayan D.
dc.date.accessioned2024-07-22T08:21:58Z
dc.date.available2024-07-22T08:21:58Z
dc.date.issued2009
dc.description.abstractThe glutathione-s-transferases are a family of multifunctional enzymes involved in the detoxification of electrophilic xenobiotics primarily through conjugation to reduce glutathione. A form of the enzyme, designated GSH-S transferase ρ, was purified chicken erythrocyte by acetone precipitation, ethanol-chloroform treatment, DEAE-Cellulose, Q-Sepharose, Sephadex G-100 chromatography. The molecular weight of GST purified from chicken erythrocyte was estimated as 47,500 Da by gel filtration. The subunit molecular weight of chicken erythrocyte GST as determined by electrophoresis in the presence of sodium dodecyl sulfate was predicted as 24,000 Da. The specific activity was found to be 20.39 U/mg. The km for CDNB calculated from Lineweaver-Burk plot was 0.71 mM. Optimum temperature of maximum GST activity was 28°C for CDNB. The maximal activity of the enzyme was observed at pH 7.5. The activity of purified GST is inhibited by DDT, urea, CDNB, Triton X-100, DTNB. Copyright © 2009 Informa UK Ltd.
dc.identifier.DOI-ID10.1080/10731190902742489
dc.identifier.issn15324184
dc.identifier.urihttp://akademikarsiv.cbu.edu.tr:4000/handle/123456789/18866
dc.language.isoEnglish
dc.rightsAll Open Access; Bronze Open Access
dc.subjectAcetone
dc.subjectAnimals
dc.subjectChickens
dc.subjectChromatography, DEAE-Cellulose
dc.subjectDDT
dc.subjectDithionitrobenzoic Acid
dc.subjectEnzyme Activation
dc.subjectErythrocytes
dc.subjectGlutathione Transferase
dc.subjectHydrogen-Ion Concentration
dc.subjectMolecular Weight
dc.subjectOctoxynol
dc.subjectPrecipitation
dc.subjectTemperature
dc.subjectUrea
dc.subjectAcetone
dc.subjectBiochemistry
dc.subjectChromatographic analysis
dc.subjectDetoxification
dc.subjectElectrophoresis
dc.subjectEnzyme activity
dc.subjectEthanol
dc.subjectGel permeation chromatography
dc.subjectGelation
dc.subjectIon exchange
dc.subjectMeats
dc.subjectMolecular weight
dc.subjectPurification
dc.subjectSodium
dc.subjectSodium sulfate
dc.subjectSystem theory
dc.subjectUrea
dc.subjectalcohol
dc.subjectchloroform
dc.subjectdiethylaminoethyl cellulose
dc.subjectdodecyl sulfate sodium
dc.subjectglutathione transferase
dc.subjectsephadex
dc.subjectsepharose
dc.subjectChicken erythrocyte
dc.subjectChloroform treatments
dc.subjectGel filtrations
dc.subjectGlutathione
dc.subjectGlutathione-S-transferase
dc.subjectInhibitors
dc.subjectLineweaver-Burk plots
dc.subjectOptimum temperatures
dc.subjectQ-sepharose
dc.subjectSephadex
dc.subjectSodium dodecyl sulfates
dc.subjectSpecific activities
dc.subjectTriton x-100
dc.subjectacid precipitation
dc.subjectanimal cell
dc.subjectarticle
dc.subjectchromatography
dc.subjectdetoxification
dc.subjectelectrophoresis
dc.subjectenzyme activity
dc.subjectenzyme analysis
dc.subjectenzyme purification
dc.subjectenzyme specificity
dc.subjecterythrocyte
dc.subjectgel filtration
dc.subjectmolecular weight
dc.subjectnonhuman
dc.subjectpolyacrylamide gel electrophoresis
dc.subjectprediction
dc.subjectprotein family
dc.subjectxenobiotic metabolism
dc.subjectEnzymes
dc.titlePurification and characterization of glutathione-S-transferase from chicken erythrocyte
dc.typeArticle

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