pubmed-article:18283 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18283 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
pubmed-article:18283 | lifeskim:mentions | umls-concept:C0005220 | lld:lifeskim |
pubmed-article:18283 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:18283 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:18283 | pubmed:dateCreated | 1977-9-17 | lld:pubmed |
pubmed-article:18283 | pubmed:abstractText | The binding of a series of alkyl 1-thio-beta-D-galactopyranosides to beta-D-galactosidase from E. coli has been investigated. The inhibition constants were compared to the partition coefficients for the transfer of these substrate-analogues from water to 1-octanol. The relationships between the observed binding-constants and the partition coefficients indicate that part of the aglycon group binds to a hydrophobic area that is limited in relation to the length of hydrocarbon chain that can be accomodated. Outside this area, the hydrocarbon chain is only partially desolvated. The main driving-force for binding of the aglycon group is the increase in entropy resulting from the return of water molecules from the more-organized layer around the solute molecule to the bulk-water phase. | lld:pubmed |
pubmed-article:18283 | pubmed:language | eng | lld:pubmed |
pubmed-article:18283 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18283 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18283 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18283 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18283 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18283 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18283 | pubmed:month | Jun | lld:pubmed |
pubmed-article:18283 | pubmed:issn | 0008-6215 | lld:pubmed |
pubmed-article:18283 | pubmed:author | pubmed-author:De BruyneC... | lld:pubmed |
pubmed-article:18283 | pubmed:author | pubmed-author:YdeMM | lld:pubmed |
pubmed-article:18283 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:18283 | pubmed:volume | 56 | lld:pubmed |
pubmed-article:18283 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18283 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18283 | pubmed:pagination | 153-64 | lld:pubmed |
pubmed-article:18283 | pubmed:dateRevised | 2000-12-18 | lld:pubmed |
pubmed-article:18283 | pubmed:meshHeading | pubmed-meshheading:18283-Hy... | lld:pubmed |
pubmed-article:18283 | pubmed:meshHeading | pubmed-meshheading:18283-Te... | lld:pubmed |
pubmed-article:18283 | pubmed:meshHeading | pubmed-meshheading:18283-Ma... | lld:pubmed |
pubmed-article:18283 | pubmed:meshHeading | pubmed-meshheading:18283-Ki... | lld:pubmed |
pubmed-article:18283 | pubmed:meshHeading | pubmed-meshheading:18283-Ga... | lld:pubmed |
pubmed-article:18283 | pubmed:meshHeading | pubmed-meshheading:18283-Es... | lld:pubmed |
pubmed-article:18283 | pubmed:meshHeading | pubmed-meshheading:18283-Pr... | lld:pubmed |
pubmed-article:18283 | pubmed:meshHeading | pubmed-meshheading:18283-St... | lld:pubmed |
pubmed-article:18283 | pubmed:meshHeading | pubmed-meshheading:18283-Th... | lld:pubmed |
pubmed-article:18283 | pubmed:meshHeading | pubmed-meshheading:18283-Th... | lld:pubmed |
pubmed-article:18283 | pubmed:year | 1977 | lld:pubmed |
pubmed-article:18283 | pubmed:articleTitle | Binding of alkyl 1-thio-beta-D-galactopyranosides to beta-D-galactosidase from E. coli. | lld:pubmed |
pubmed-article:18283 | pubmed:publicationType | Journal Article | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18283 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18283 | lld:pubmed |