| pubmed-article:150841 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:150841 | lifeskim:mentions | umls-concept:C0596533 | lld:lifeskim |
| pubmed-article:150841 | lifeskim:mentions | umls-concept:C0024467 | lld:lifeskim |
| pubmed-article:150841 | lifeskim:mentions | umls-concept:C0080194 | lld:lifeskim |
| pubmed-article:150841 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:150841 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
| pubmed-article:150841 | lifeskim:mentions | umls-concept:C0205349 | lld:lifeskim |
| pubmed-article:150841 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:150841 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:150841 | pubmed:dateCreated | 1978-10-25 | lld:pubmed |
| pubmed-article:150841 | pubmed:abstractText | Membranes from a mutant strain of Escherichia coli K12 carrying the uncD409 allele were washed in low-ionic-strength buffers in the presence or absence of the proteinase inhibitor p-aminobenzamidine. Unlike membranes from a normal strain, those from strain AN463 (uncD409) did not become proton-permeable, as judged by NADH-induced atebrinfluorescence quenching, when the membranes were washed in the absence of p-aminobenzamide. Furthermore, ATP-dependent atebrin-fluorscence quenching in such washed membranes could not be reconstituted by the addition of solubilized Mg2+-stimulated adenosine triphosphatase preparations. The examination by two-dimensional polyacrylamide-gel electrophoresis of the polypeptide composition of the washed membranes from strain AN463 (uncD409) indicated the presence of a polypeptide of similar molecular weight to the normal beta-subunit of the Mg2+-stimulated adenosine triphosphatase, but with an altered isoelectric point. Both the normal and abnormal beta-subunits were identified in membranes prepared from a partial diploid strain carrying both the unc+ and uncD409 alleles. It is concluded that the uncD gene codes for the beta-subunit of the Mg2+-stimulated adenosine triphosphatase. | lld:pubmed |
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| pubmed-article:150841 | pubmed:language | eng | lld:pubmed |
| pubmed-article:150841 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:150841 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:150841 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:150841 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:150841 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:150841 | pubmed:author | pubmed-author:DownieJ AJA | lld:pubmed |
| pubmed-article:150841 | pubmed:author | pubmed-author:RAOS RSR | lld:pubmed |
| pubmed-article:150841 | pubmed:author | pubmed-author:GibsonFF | lld:pubmed |
| pubmed-article:150841 | pubmed:author | pubmed-author:FayleD RDR | lld:pubmed |
| pubmed-article:150841 | pubmed:author | pubmed-author:RadikJJ | lld:pubmed |
| pubmed-article:150841 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:150841 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:150841 | pubmed:volume | 172 | lld:pubmed |
| pubmed-article:150841 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:150841 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:150841 | pubmed:pagination | 523-31 | lld:pubmed |
| pubmed-article:150841 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:150841 | pubmed:meshHeading | pubmed-meshheading:150841-A... | lld:pubmed |
| pubmed-article:150841 | pubmed:year | 1978 | lld:pubmed |
| pubmed-article:150841 | pubmed:articleTitle | Characterization of the mutant-unc D-gene product in a strain of Escherichia coli K12. An altered beta-subunit of the magnesium ion-stimulated adenosine triphosphatase. | lld:pubmed |
| pubmed-article:150841 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:150841 | pubmed:publicationType | In Vitro | lld:pubmed |
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