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dc.contributor.authorAdem, S. and Ciftci, M.
dc.date.accessioned2021-04-08T12:08:27Z
dc.date.available2021-04-08T12:08:27Z
dc.date.issued2016
dc.identifier10.3109/14756366.2015.1132711
dc.identifier.issn14756366
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84954284952&doi=10.3109%2f14756366.2015.1132711&partnerID=40&md5=1d6c53edbddcefdd63f0491d603b5d8c
dc.identifier.urihttp://acikerisim.bingol.edu.tr/handle/20.500.12898/4606
dc.description.abstractG6PD, 6PGD and GR have been purified separately in the single step from rat lung using 2′, 5′-ADP Sepharose 4B affinity chromatography. The purified enzymes showed a single band on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weights of the enzymes were estimated to be 134 kDa for G6PD, 107 kDa for 6PGD and 121 kDa for GR by Sephadex G-150 gel filtration chromatography, and the subunit molecular weights was respectively found to be 66, 52 and 63 kDa by SDS-PAGE. Optimum pH, stable pH, optimum ionic strength, optimum temperature, KM and V max values for substrates were determined. Product inhibition studies were also performed. The enzymes were inhibited by levofloxacin, furosemide, ceftazidime, cefuroxime and gentamicin as in vitro with IC50 values in the range of 0.07–30.13 mM. In vivo studies demonstrated that lung GR was inhibited by furosemide and lung 6PGD was inhibited by levofloxacin. © 2016 Informa UK Limited, trading as Taylor & Francis Group.
dc.language.isoEnglish
dc.sourceJournal of Enzyme Inhibition and Medicinal Chemistry
dc.titlePurification and biochemical characterization of glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glutathione reductase from rat lung and inhibition effects of some antibiotics


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