| pubmed-article:4153028 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:4153028 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:4153028 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
| pubmed-article:4153028 | lifeskim:mentions | umls-concept:C1706373 | lld:lifeskim |
| pubmed-article:4153028 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:4153028 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:4153028 | lifeskim:mentions | umls-concept:C0205254 | lld:lifeskim |
| pubmed-article:4153028 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:4153028 | pubmed:dateCreated | 1974-11-18 | lld:pubmed |
| pubmed-article:4153028 | pubmed:abstractText | The Mg(2+)- and Ca(2+)-stimulated ATPase (EC 3.6.1.3; ATP phosphohydrolase) (bacterial coupling factor) was purified from two strains of E. coli by two different procedures: (a) method of Nelson, Kanner, and Gutnick [Proc. Nat. Acad. Sci. USA (1974) 71, 2720-2724] and (b) a modified procedure described in this paper. The ATPase purified from E. coli K12 (lambda) by the first procedure had 4 subunits (alpha, beta, gamma, and epsilon). It did not bind to a deficient membrane, nor did it reconstitute ATP-driven transhydrogenase activity. Our modified procedure (b) yielded 5 subunits (alpha, beta, gamma, delta, and epsilon). This ATPase could bind to a deficient membrane and reconstitute ATP-driven transhydrogenase. This finding suggests that the delta subunit is required for the reaction with the membrane. The molecular weight of the 4-subunit ATPase was significantly lower than that of the 5-subunit ATPase, as judged by equilibrium centrifugation. The specific ATPase activities of both preparations were about the same. These two procedures were also applied to E. coli ML308-225. | lld:pubmed |
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| pubmed-article:4153028 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:4153028 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:4153028 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:4153028 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:4153028 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:4153028 | pubmed:author | pubmed-author:HeppelL ALA | lld:pubmed |
| pubmed-article:4153028 | pubmed:author | pubmed-author:FutaiMM | lld:pubmed |
| pubmed-article:4153028 | pubmed:author | pubmed-author:SternweisP... | lld:pubmed |
| pubmed-article:4153028 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:4153028 | pubmed:volume | 71 | lld:pubmed |
| pubmed-article:4153028 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:4153028 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:4153028 | pubmed:pagination | 2725-9 | lld:pubmed |
| pubmed-article:4153028 | pubmed:dateRevised | 2010-9-10 | lld:pubmed |
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| pubmed-article:4153028 | pubmed:year | 1974 | lld:pubmed |
| pubmed-article:4153028 | pubmed:articleTitle | Purification and properties of reconstitutively active and inactive adenosinetriphosphatase from Escherichia coli. | lld:pubmed |
| pubmed-article:4153028 | pubmed:publicationType | Journal Article | lld:pubmed |
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