Purification of glutathione S-transferase isoenzymes from tumour and nontumour human stomach and inhibitory effects of some heavy metals on enzymes activities

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dc.contributor.authorDemirdag, Ramazan
dc.contributor.authorYerlikaya, Emrah
dc.contributor.authorKufrevioglu, Omer Irfan
dc.contributor.authorGundogdu, Cemal
dc.date.accessioned2019-11-18T10:14:27Z
dc.date.available2019-11-18T10:14:27Z
dc.date.issued2013-04
dc.departmentBelirleneceken_US
dc.description.abstractIn this study, glutathione S-transferase (GST) enzyme was purified from nontumour and tumour human gastric tissue and in vitro effects of heavy metals on the enzyme were examined. GST was purified 3089 fold with a specific activity of 20 U/mg and a yield of 78% from gastric tumour tissue; and 1185 fold with a specific activity of 5.69 U/mg and a yield of 50% from nontumour tissue by using glutathione-agarose affinity column, respectively. Enzyme purity was verified by SDS-PAGE and subunit molecular mass was calculated around 26 kDa. The molecular weight of the enzyme was calculated as 52 kDa by using Sephadex G-75 gel filtration column. Then, inhibitory effects of metal ions on the enzymes were investigated. Mg2+ and Cd2+ had inhibitory effect on the enzymes activities. Other kinetic properties of the enzymes were also determined.en_US
dc.identifier.issn1475-6366
dc.identifier.urihttps://hdl.handle.net/20.500.12604/1611
dc.language.isoenen_US
dc.relation.publicationcategoryUluslararası Hakemli Dergi Makalesien_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.snmz#KayıtKontrol#
dc.subjectCancer, GST, enzyme, metal, inhibitionen_US
dc.titlePurification of glutathione S-transferase isoenzymes from tumour and nontumour human stomach and inhibitory effects of some heavy metals on enzymes activitiesen_US
dc.typeArticleen_US

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