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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1985-12-11
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pubmed:abstractText |
NAD-dependent formate dehydrogenase (EC 1.2.1.2), was isolated from the methanol-utilizing yeast Candida methylica. Two purification techniques for the enzyme from the crude yeast extract have been developed: a two-step procedure, involving a sequential application of DEAE-cellulose ion-exchange chromatography and Sephadex G-200 gel filtration, and a single-step procedure, preparative isoelectric focusing in a granulated gel layer. The enzyme proved to be electrophoretically homogeneous. It consisted of two identical subunits with a relative molecular mass of 46 000, each containing one -SH group related to manifestation of the catalytic activity. The Michaelis constant was 1 X 10(-4) M for NAD and 1.3 X 10(-2) M for formate. Formate dehydrogenase was inhibited with p-chlormercuribenzoate, iodoacetamide, dithionitrobenzoate, cyanide and azide.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
152
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
657-62
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:4054127-Aldehyde Oxidoreductases,
pubmed-meshheading:4054127-Candida,
pubmed-meshheading:4054127-Chromatography, DEAE-Cellulose,
pubmed-meshheading:4054127-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:4054127-Formate Dehydrogenases,
pubmed-meshheading:4054127-Hydrogen-Ion Concentration,
pubmed-meshheading:4054127-Isoelectric Focusing,
pubmed-meshheading:4054127-Molecular Weight,
pubmed-meshheading:4054127-NAD,
pubmed-meshheading:4054127-Substrate Specificity,
pubmed-meshheading:4054127-Sulfhydryl Compounds
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pubmed:year |
1985
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pubmed:articleTitle |
Biosynthesis, isolation and properties of NAD-dependent formate dehydrogenase from the yeast Candida methylica.
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pubmed:publicationType |
Journal Article
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