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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1985-5-23
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pubmed:abstractText |
A soluble oxidase from phorbol-stimulated pig neutrophils contained FAD and cytochrome b-245. A typical preparation produced 13.03 mol of superoxide (O2-.) X S-1 X mol of cytochrome b-1 (348 nmol X min-1 X mg of protein-1). In the aerobic steady state, cytochrome b was 8.9% reduced. Steady-state cytochrome b reduction was absent from extracts of unstimulated cells; Km values for NADPH, for O2-. production and cytochrome b reduction were similar. The calculated aerobic rate of cytochrome b reduction was equal to the measured rate of O2-. production in a variety of preparations and in the presence of a range of inhibitors. Under anaerobic conditions the rate was slow: O2 is apparently required for rapid electron flow into the oxidase complex. Cytochrome b is shown to be kinetically competent to act as part of the O2-.-generating complex.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2985050-13654378,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2985050-198771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2985050-216707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2985050-24176,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2985050-6261795,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2985050-6279625,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2985050-6293459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2985050-6497852,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2985050-6848934,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2985050-7115343,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2985050-7116949,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2985050-7306004,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2985050-9426
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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 |
Mar
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
226
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
881-4
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pubmed:dateRevised |
2010-9-10
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pubmed:meshHeading |
pubmed-meshheading:2985050-Animals,
pubmed-meshheading:2985050-Cytochrome b Group,
pubmed-meshheading:2985050-Dithionite,
pubmed-meshheading:2985050-Kinetics,
pubmed-meshheading:2985050-NADH, NADPH Oxidoreductases,
pubmed-meshheading:2985050-NADP,
pubmed-meshheading:2985050-NADPH Oxidase,
pubmed-meshheading:2985050-Neutrophils,
pubmed-meshheading:2985050-Oxidation-Reduction,
pubmed-meshheading:2985050-Oxygen,
pubmed-meshheading:2985050-Spectrophotometry,
pubmed-meshheading:2985050-Superoxides,
pubmed-meshheading:2985050-Swine
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pubmed:year |
1985
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pubmed:articleTitle |
Mechanism of the superoxide-producing oxidase of neutrophils. O2 is necessary for the fast reduction of cytochrome b-245 by NADPH.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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