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pubmed-article:2147417pubmed:abstractTextThe 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
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pubmed-article:2147417pubmed:dateRevised2007-7-23lld:pubmed
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pubmed-article:2147417pubmed:articleTitleReconstitution of CF0F1 into liposomes using a new reconstitution procedure.lld:pubmed
pubmed-article:2147417pubmed:affiliationMax-Volmer-Institut, Technische Universität Berlin, Federal Republic of Germany.lld:pubmed
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pubmed-article:2147417pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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