pubmed-article:3519632 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3519632 | lifeskim:mentions | umls-concept:C0001942 | lld:lifeskim |
pubmed-article:3519632 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:3519632 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:3519632 | lifeskim:mentions | umls-concept:C1564799 | lld:lifeskim |
pubmed-article:3519632 | lifeskim:mentions | umls-concept:C0053858 | lld:lifeskim |
pubmed-article:3519632 | pubmed:dateCreated | 1986-7-17 | lld:pubmed |
pubmed-article:3519632 | 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. | lld:pubmed |
pubmed-article:3519632 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3519632 | pubmed:language | eng | lld:pubmed |
pubmed-article:3519632 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3519632 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3519632 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3519632 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3519632 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3519632 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3519632 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3519632 | pubmed:month | Apr | lld:pubmed |
pubmed-article:3519632 | pubmed:issn | 0021-9673 | lld:pubmed |
pubmed-article:3519632 | pubmed:author | pubmed-author:StellwagenEE | lld:pubmed |
pubmed-article:3519632 | pubmed:author | pubmed-author:LiuY CYC | lld:pubmed |
pubmed-article:3519632 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3519632 | pubmed:day | 11 | lld:pubmed |
pubmed-article:3519632 | pubmed:volume | 376 | lld:pubmed |
pubmed-article:3519632 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3519632 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3519632 | pubmed:pagination | 149-55 | lld:pubmed |
pubmed-article:3519632 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:3519632 | pubmed:meshHeading | pubmed-meshheading:3519632-... | lld:pubmed |
pubmed-article:3519632 | pubmed:year | 1986 | lld:pubmed |
pubmed-article:3519632 | pubmed:articleTitle | Zonal chromatographic analysis of the interaction of alcohol dehydrogenase with blue-sepharose. | lld:pubmed |
pubmed-article:3519632 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3519632 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |