pubmed-article:2147417 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2147417 | lifeskim:mentions | umls-concept:C0023828 | lld:lifeskim |
pubmed-article:2147417 | lifeskim:mentions | umls-concept:C0184661 | lld:lifeskim |
pubmed-article:2147417 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:2147417 | pubmed:dateCreated | 1991-1-11 | lld:pubmed |
pubmed-article:2147417 | pubmed:abstractText | The H(+)-ATPase (ATP synthase) from chloroplasts was isolated, purified and reconstituted into phosphatidylcholine/phosphatidic-acid liposomes. Liposomes prepared by reverse-phase evaporation were treated with various amounts of Triton X-100 and protein incorporation was studied at each step of the solubilization process. After detergent removal by SM2-Biobeads, the activities of the resulting proteoliposomes were measured indicating that the most efficient reconstitution was obtained by insertion of the protein into preformed, detergent-saturated liposomes. The conditions for the reconstitution were optimized with regard to ATP synthesis driven by an artificially generated delta pH/delta psi. An important benefit of the new reconstituted CF0F1 liposomes is the finding that the rate of ATP synthesis remains constant up to 10 s, indicating a low basal membrane permeability. | lld:pubmed |
pubmed-article:2147417 | pubmed:language | eng | lld:pubmed |
pubmed-article:2147417 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2147417 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2147417 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2147417 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2147417 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2147417 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2147417 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2147417 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2147417 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2147417 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2147417 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2147417 | pubmed:month | Nov | lld:pubmed |
pubmed-article:2147417 | pubmed:issn | 0014-2956 | lld:pubmed |
pubmed-article:2147417 | pubmed:author | pubmed-author:RichardPP | lld:pubmed |
pubmed-article:2147417 | pubmed:author | pubmed-author:GräberPP | lld:pubmed |
pubmed-article:2147417 | pubmed:author | pubmed-author:RigaudJ LJL | lld:pubmed |
pubmed-article:2147417 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2147417 | pubmed:day | 13 | lld:pubmed |
pubmed-article:2147417 | pubmed:volume | 193 | lld:pubmed |
pubmed-article:2147417 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2147417 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2147417 | pubmed:pagination | 921-5 | lld:pubmed |
pubmed-article:2147417 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
pubmed-article:2147417 | pubmed:meshHeading | pubmed-meshheading:2147417-... | lld:pubmed |
pubmed-article:2147417 | pubmed:meshHeading | pubmed-meshheading:2147417-... | lld:pubmed |
pubmed-article:2147417 | pubmed:meshHeading | pubmed-meshheading:2147417-... | lld:pubmed |
pubmed-article:2147417 | pubmed:meshHeading | pubmed-meshheading:2147417-... | lld:pubmed |
pubmed-article:2147417 | pubmed:meshHeading | pubmed-meshheading:2147417-... | lld:pubmed |
pubmed-article:2147417 | pubmed:meshHeading | pubmed-meshheading:2147417-... | lld:pubmed |
pubmed-article:2147417 | pubmed:meshHeading | pubmed-meshheading:2147417-... | lld:pubmed |
pubmed-article:2147417 | pubmed:meshHeading | pubmed-meshheading:2147417-... | lld:pubmed |
pubmed-article:2147417 | pubmed:meshHeading | pubmed-meshheading:2147417-... | lld:pubmed |
pubmed-article:2147417 | pubmed:meshHeading | pubmed-meshheading:2147417-... | lld:pubmed |
pubmed-article:2147417 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2147417 | pubmed:articleTitle | Reconstitution of CF0F1 into liposomes using a new reconstitution procedure. | lld:pubmed |
pubmed-article:2147417 | pubmed:affiliation | Max-Volmer-Institut, Technische Universität Berlin, Federal Republic of Germany. | lld:pubmed |
pubmed-article:2147417 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2147417 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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