| pubmed-article:2512991 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2512991 | lifeskim:mentions | umls-concept:C0596533 | lld:lifeskim |
| pubmed-article:2512991 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:2512991 | lifeskim:mentions | umls-concept:C1151379 | lld:lifeskim |
| pubmed-article:2512991 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:2512991 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2512991 | pubmed:dateCreated | 1990-1-29 | lld:pubmed |
| pubmed-article:2512991 | pubmed:abstractText | We used an anti-trimethylamine-N-oxide reductase (EC 1.6.6.9) serum and different immunological techniques (Ouchterlony, rocket immunoelectrophoresis, immunoblotting) to show that dimethylsulphoxide (DMSO), tetrahydrothiophene 1-oxide (THTO) and pyridine N-oxide (PNO) were effective inducers of the inducible form of trimethylamine N-oxide reductase. We confirmed this genetically and biochemically using a strain in which phage MudII 1734 carrying lacZ was inserted into torA, the structural gene for inducible trimethylamine-N-oxide reductase. By subcellular fractionation and quantitation with rocket immunoelectrophoresis, we showed that the enzyme was principally localized in the periplasmic fraction. Constitutive trimethylamine-N-oxide reductase was localized in the membrane fraction and, like the inducible enzyme showed a broad specificity with respect to various compounds such as DMSO, THTO and PNO. Apart from their immunological properties, the two enzymes could be clearly differentiated by their temperature stability. | lld:pubmed |
| pubmed-article:2512991 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2512991 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2512991 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2512991 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2512991 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:2512991 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:2512991 | pubmed:author | pubmed-author:PommierJJ | lld:pubmed |
| pubmed-article:2512991 | pubmed:author | pubmed-author:PascalM CMC | lld:pubmed |
| pubmed-article:2512991 | pubmed:author | pubmed-author:GiordanoGG | lld:pubmed |
| pubmed-article:2512991 | pubmed:author | pubmed-author:SilvestroAA | lld:pubmed |
| pubmed-article:2512991 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2512991 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:2512991 | pubmed:volume | 999 | lld:pubmed |
| pubmed-article:2512991 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2512991 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2512991 | pubmed:pagination | 208-16 | lld:pubmed |
| pubmed-article:2512991 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:2512991 | pubmed:meshHeading | pubmed-meshheading:2512991-... | lld:pubmed |
| pubmed-article:2512991 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2512991 | pubmed:articleTitle | The inducible trimethylamine N-oxide reductase of Escherichia coli K12: its localization and inducers. | lld:pubmed |
| pubmed-article:2512991 | pubmed:affiliation | Centre National de la Recherche Scientifique, Département de Biologie, Faculté des Sciences de Luminy, Marseille, France. | lld:pubmed |
| pubmed-article:2512991 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2512991 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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