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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1983-10-8
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pubmed:abstractText |
Copper (Cu2+) ions at physiological concentrations can promote the formation of hydroxyl radical (OH) or a species of equivalent reactivity. The reaction requires H2O2 and a reducing agent. Reduction of Cu2+ can be achieved by superoxide ion generated by a mixture of hypoxanthine and xanthine oxidase or added directly as its potassium salt. Reduction of Cu2+ can also be achieved by ascorbic acid. Hence both O2- -dependent and ascorbate-dependent formation of OH from H2O2 in the presence of Cu2+ can be observed. Only the former reaction is significantly inhibited by superoxide dismutase. The binding of Cu2+ to histidine or albumin at physiological concentrations decreases the formation of OH radicals in free solution in the presence of either ascorbate or an (O2- -generating system. It is suggested that OH is still formed but reacts immediately with the binding molecule.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0003-9861
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
225
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
279-84
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:6311105-Ascorbic Acid,
pubmed-meshheading:6311105-Chemical Phenomena,
pubmed-meshheading:6311105-Chemistry,
pubmed-meshheading:6311105-Copper,
pubmed-meshheading:6311105-Enzyme Inhibitors,
pubmed-meshheading:6311105-Free Radicals,
pubmed-meshheading:6311105-Hydrogen Peroxide,
pubmed-meshheading:6311105-Hydroxides,
pubmed-meshheading:6311105-Hydroxyl Radical,
pubmed-meshheading:6311105-Oxygen,
pubmed-meshheading:6311105-Protein Binding,
pubmed-meshheading:6311105-Superoxides
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pubmed:year |
1983
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pubmed:articleTitle |
Superoxide-dependent and ascorbate-dependent formation of hydroxyl radicals in the presence of copper salts: a physiologically significant reaction?
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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