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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1986-7-17
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pubmed:abstractText |
The interaction between horse liver alcohol dehydrogenase and Reactive blue 2 immobilized on Sepharose CL-6B was measured by zonal chromatography. Each protein molecule was retained by a single immobilized dye using a Blue-Sepharose column containing a total of 1.38 mM dye. However, the protein was predominantly retained by two immobilized dye molecules using a darker Blue-Sepharose column containing a total of 11.6 mM dye. The dissociation constant measured for the alcohol dehydrogenase--immobilized dye complex on each column is identical to the inhibition constant for the alcohol dehydrogenase--free Reactive blue 2 complex: 4.5 +/- 0.8 microM.
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pubmed:grant | |
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 |
Apr
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pubmed:issn |
0021-9673
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
376
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
149-55
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3519632-Alcohol Oxidoreductases,
pubmed-meshheading:3519632-Animals,
pubmed-meshheading:3519632-Catalysis,
pubmed-meshheading:3519632-Chromatography, Agarose,
pubmed-meshheading:3519632-Horses,
pubmed-meshheading:3519632-Liver,
pubmed-meshheading:3519632-NAD,
pubmed-meshheading:3519632-Sepharose
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pubmed:year |
1986
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pubmed:articleTitle |
Zonal chromatographic analysis of the interaction of alcohol dehydrogenase with blue-sepharose.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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