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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1987-10-30
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pubmed:abstractText |
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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/5,5-dimethyl-1-pyrroline-1-oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Copper,
http://linkedlifedata.com/resource/pubmed/chemical/Copper Sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic N-Oxides,
http://linkedlifedata.com/resource/pubmed/chemical/Free Radicals,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxides,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxyl Radical,
http://linkedlifedata.com/resource/pubmed/chemical/Nitroblue Tetrazolium,
http://linkedlifedata.com/resource/pubmed/chemical/Spin Labels,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxides,
http://linkedlifedata.com/resource/pubmed/chemical/Xanthine,
http://linkedlifedata.com/resource/pubmed/chemical/Xanthine Oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Xanthines
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
915
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
267-76
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2820500-Animals,
pubmed-meshheading:2820500-Cattle,
pubmed-meshheading:2820500-Copper,
pubmed-meshheading:2820500-Copper Sulfate,
pubmed-meshheading:2820500-Cyclic N-Oxides,
pubmed-meshheading:2820500-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:2820500-Free Radicals,
pubmed-meshheading:2820500-Hydroxides,
pubmed-meshheading:2820500-Hydroxyl Radical,
pubmed-meshheading:2820500-Nitroblue Tetrazolium,
pubmed-meshheading:2820500-Oxidation-Reduction,
pubmed-meshheading:2820500-Spin Labels,
pubmed-meshheading:2820500-Superoxide Dismutase,
pubmed-meshheading:2820500-Superoxides,
pubmed-meshheading:2820500-Xanthine,
pubmed-meshheading:2820500-Xanthine Oxidase,
pubmed-meshheading:2820500-Xanthines
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pubmed:year |
1987
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pubmed:articleTitle |
Superoxide dismutase-like activities of copper(II) complexes tested in serum.
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pubmed:affiliation |
Department of Basic Pharmaceutical Sciences, University of South Carolina, Columbia 29208.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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