pubmed-article:4565537 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:4565537 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
pubmed-article:4565537 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
pubmed-article:4565537 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
pubmed-article:4565537 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
pubmed-article:4565537 | lifeskim:mentions | umls-concept:C1701901 | lld:lifeskim |
pubmed-article:4565537 | lifeskim:mentions | umls-concept:C0064530 | lld:lifeskim |
pubmed-article:4565537 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:4565537 | pubmed:dateCreated | 1973-2-15 | lld:pubmed |
pubmed-article:4565537 | pubmed:abstractText | A temperature-sensitive mutant of Escherichia coli in which the synthesis of l-arabinose isomerase is blocked during growth at 42 C was found to possess the following properties. (i) The mutation occurred in the structural gene for the isomerase, gene araA. (ii) During growth at elevated temperatures the mutant accumulates a product which is a precursor to the active enzyme. (iii) The precursor produced at 42 C is slowly converted to active enzyme at 28 C in the absence of protein and ribonucleic acid synthesis. It is concluded that the mutation results in a change in the structure of isomerase which causes formation of active enzyme to be thermolabile at a step beyond the level of translation. | lld:pubmed |
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pubmed-article:4565537 | pubmed:language | eng | lld:pubmed |
pubmed-article:4565537 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:4565537 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:4565537 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:4565537 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:4565537 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:4565537 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:4565537 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:4565537 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:4565537 | pubmed:month | Dec | lld:pubmed |
pubmed-article:4565537 | pubmed:issn | 0021-9193 | lld:pubmed |
pubmed-article:4565537 | pubmed:author | pubmed-author:IrrJJ | lld:pubmed |
pubmed-article:4565537 | pubmed:author | pubmed-author:PauleyJJ | lld:pubmed |
pubmed-article:4565537 | pubmed:author | pubmed-author:PowerJJ | lld:pubmed |
pubmed-article:4565537 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:4565537 | pubmed:volume | 112 | lld:pubmed |
pubmed-article:4565537 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:4565537 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:4565537 | pubmed:pagination | 1247-53 | lld:pubmed |
pubmed-article:4565537 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:4565537 | pubmed:year | 1972 | lld:pubmed |
pubmed-article:4565537 | pubmed:articleTitle | L-arabinose isomerase formation in a conditional mutant of gene araA of Escherichia coli B-r. | lld:pubmed |
pubmed-article:4565537 | pubmed:publicationType | Journal Article | lld:pubmed |