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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
|
pubmed:dateCreated |
1984-2-24
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pubmed:abstractText |
Nitrite reductase from Clostridium perfringens was purified by chromatographies on DEAE-cellulose, DEAE-Sephadex, Sephadex G-150, and hydroxylapatite and by isoelectric focussing to a homogeneous state, showing essentially a single protein band in disc gel electrophoresis and a single immuno-precipitation line in double diffusion against antiserum obtained from immunized rabbits. The reductase was induced in the presence of nitrate. It had a molecular weight of 54,000 and showed no absorption peak in the visible region. The pH optimum was 6.2 and Km for nitrite was 5 mM. Ferredoxin, as well as viologen dyes, was found to be an electron donor. The product of nitrite reduction was hydroxylamine. This reductase was inhibited by o-phenanthroline and azide but not by cyanide or diethyldithiocarbamate.
|
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-924X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
94
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
1053-9
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pubmed:dateRevised |
2007-12-19
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pubmed:meshHeading |
pubmed-meshheading:6317661-Clostridium perfringens,
pubmed-meshheading:6317661-Electron Transport,
pubmed-meshheading:6317661-Immunodiffusion,
pubmed-meshheading:6317661-Kinetics,
pubmed-meshheading:6317661-Molecular Weight,
pubmed-meshheading:6317661-NADH, NADPH Oxidoreductases,
pubmed-meshheading:6317661-Nitrite Reductases,
pubmed-meshheading:6317661-Species Specificity
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pubmed:year |
1983
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pubmed:articleTitle |
Purification and some properties of nitrite reductase from Clostridium perfringens.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|