Please use this identifier to cite or link to this item:
http://hdl.handle.net/20.500.11889/3943
DC Field | Value | Language |
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dc.contributor.author | Abu Hijleh, Abdullatif | - |
dc.date.accessioned | 2016-12-14T12:00:02Z | - |
dc.date.available | 2016-12-14T12:00:02Z | - |
dc.date.issued | 2010 | - |
dc.identifier.uri | http://hdl.handle.net/20.500.11889/3943 | - |
dc.description.abstract | The superoxide dismutase-like activities of a series of coordination complexes of copper were evaluated and compared to the activities of bovine erythrocyte superoxide dismutase (superoxide: superoxide oxidoreductase, EC 1.15.1.1) in serum using the nitroblue tetrazolium chloride (NBT)-reduction assay and electron paramagnetic resonance (EPR) spectroscopy. A 40% inhibition was observed for the initial rate of the NBT reduction by superoxide dismutase in serum, but more than 40% inhibition was achieved with CuSO4, Cu(II)-dimethylglyoxime, Cu(II)-3,8-dimethyl-4,7-diazadeca-3,7-dienediamide, Cu2[N,N'-(2-(O-hydroxy-benzhydrylidene)amino)ethyl]2-1,2-ethane dia mine), Cu(II)-(diisopropylsalicylate)2, Cu(II)-(p-bromo-benzoate)2, Cu(II)-(nicotinate)2 and Cu(II)-(1,2-diamino-2-methylpropane)2. The electron paramagnetic resonance technique of spin trapping was used to detect the formation of superoxide (O2-.) and other free radicals in the xanthine-xanthine oxidase system under a variety of conditions. Addition of the spin trapping agent 5,5-dimethylpyrroline 1-oxide (DMPO) to the xanthine-xanthine oxidase system in fetal bovine serum produced the O2-.-spin adduct of DMPO (herein referred to as superoxide spin adduct, DMPO-OOH) as the well known short-lived nitroxyl whose characteristic EPR spectrum was recorded before its rapid decay to undetectable levels. The hydroxyl radical (HO.) adduct of the spin trap DMPO (herein referred to as DMPO-OH) was detected to a very small extent. When CuSO4, or the test complexes of copper, were added to the xanthine-xanthine oxidase system in serum containing the spin trap, the yield of DMPO-OOH was negligible. In addition to their superoxide dismutase-like activity, CuSO4 and the copper complexes also behaved as Fenton-type catalysts as seen by the accumulation of varying amounts of the hydroxyl spin adduct DMPO-OH. Both the Fenton-type catalysis and the superoxide dismutase-like action of these compounds were lost when a chelator such as EDTA was included in the xanthine-xanthine oxidase incubation mixture. Addition of superoxide dismutase instead of the copper compounds to this enzyme system abolished the formation of superoxide adduct DMPO-OOH, and no hydroxyl adduct DMPO-OH was detected. This effect of superoxide dismutase remained unaltered by EDTA | en_US |
dc.language.iso | en_US | en_US |
dc.subject.lcsh | Copper compounds - Physiological effect | - |
dc.subject.lcsh | Nonsteroidal anti-inflammatory agents | - |
dc.subject.lcsh | Copper compounds - Therapeutic use | - |
dc.title | Superoxide dismutase and oxidase activities of copper(II) complexes of the anti-inflammatory drug ibuprofen with imidazoles and pyrazole | en_US |
dc.type | Article | en_US |
newfileds.department | Science | en_US |
newfileds.item-access-type | open_access | en_US |
newfileds.thesis-prog | none | en_US |
newfileds.general-subject | Human Biology, Medicine and Health Sciences | الطب والعلوم الطبية | en_US |
item.fulltext | With Fulltext | - |
item.languageiso639-1 | other | - |
item.grantfulltext | open | - |
Appears in Collections: | Fulltext Publications |
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Superoxide Dismutase and Oxidase Activities of Copper (II) Complexes of the Anti-inflammatory Drug Ibuprofen with Imidazoles and Pyrazole.pdf | 169.63 kB | Adobe PDF | View/Open |
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