Alteration of enzyme activities and kinetic properties of GST and NQO1 with naturally occurring phenolic compounds

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dc.contributor.authorKarakurt, Serdar
dc.contributor.authorSever, Melike
dc.contributor.authorÇelebioğlu, Hasan Ufuk
dc.contributor.authorAdalı, Orhan
dc.date.accessioned2020-03-26T19:00:40Z
dc.date.available2020-03-26T19:00:40Z
dc.date.issued2015
dc.departmentSelçuk Üniversitesien_US
dc.description.abstractObjective: Glutathione S-transferase (GST) and NAD(P)H:quinine oxidoreductase 1 (NQO1) are the enzymes important in cytoprotection and bioactivation of chemicals. This study has addressed effects of polyphenolic compounds; ellagic acid, quercetin, naringenin, resveratrol, rutin and hesperidin on rabbit liver GST and NQO1 enzyme activities. Methods: Cytosolic fractions were obtained from homogenized liver tissues of rabbit by differential centrifugation. After calculating IC50 values of individual enzymes for phenolic compounds, both Lineweaver-Burk and Dixon plots were drawn to determine the effect of phenolics on enzyme activity. Michaelis-Menten constant (K-m), maximum velocity (V-max), and inhibition constant (K-i) were calculated from Lineweaver-Burk and Dixon plots, respectively. Results: Resveratrol was found to be the most potent inhibitor for rabbit hepatic cytosolic GST activity with 75.9 +/- 2.06 mu M IC50 value while naringenin was the least potent one with IC50 value of 260 +/- 1.92 mu M. Hesperidin and quercetin were found to be the most and least potent inhibitors for NQO1 enzyme activity with IC50 values of 2.7 +/- 0.85 mu M and 13.8 +/- 0.91 mu M, respectively. Resveratrol and naringenin inhibited GST activity noncompetitively and mixed type with K-i of 6.2 mu M and 245 mu M, respectively; while both hesperidin with 0.64 mu M K-i value and quercetin with 3.5 mu M K-i value inhibited NQO1 activity in a competitive manner. Conclusion: These results indicate that phenolic compounds may modulate Phase II enzyme, GST and NQO1. Moreover, they can influence the metabolic activation of xenobiotic and toxic compounds metabolized by this enzyme.en_US
dc.description.sponsorshipResearch Foundation of Selcuk University (BAP)Selcuk University; Research Foundation of Middle East Technical Universityen_US
dc.description.sponsorshipThis work is supported by The Research Foundation of Selcuk University (BAP) and The Research Foundation of Middle East Technical University.en_US
dc.identifier.doi10.1515/tjb-2015-0010en_US
dc.identifier.endpage257en_US
dc.identifier.issn0250-4685en_US
dc.identifier.issn1303-829Xen_US
dc.identifier.issue3en_US
dc.identifier.scopusqualityQ4en_US
dc.identifier.startpage251en_US
dc.identifier.urihttps://dx.doi.org/10.1515/tjb-2015-0010
dc.identifier.urihttps://hdl.handle.net/20.500.12395/31813
dc.identifier.volume40en_US
dc.identifier.wosWOS:000358306700008en_US
dc.identifier.wosqualityQ4en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherWALTER DE GRUYTER GMBHen_US
dc.relation.ispartofTURKISH JOURNAL OF BIOCHEMISTRY-TURK BIYOKIMYA DERGISIen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.selcuk20240510_oaigen_US
dc.subjectGSTen_US
dc.subjectNQO1en_US
dc.subjectpolyphenolsen_US
dc.subjectinhibition kineticen_US
dc.subjectIC50en_US
dc.titleAlteration of enzyme activities and kinetic properties of GST and NQO1 with naturally occurring phenolic compoundsen_US
dc.typeArticleen_US

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