rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1976-6-2
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pubmed:abstractText |
1. Oxidative phosphorylation was reconstituted with a mitochondrial proton pump (oligomycin-sensitive ATPase) and segments of the oxidation chain (cytochrome oxidase or DPNH-Q1 reductase). A proton pump of bacteriorhodopsin substituted for the respiratory chain components, giving rise to light-induced ATP formation. 2. Since oxidative phosphorylation has thus become a special case of the problem of ion translocation in general, we have investigated and reconsituted other pumps. The reconstituted Ca++ pump of sarcoplasmic reticulum consists of two factors, the Ca++-dependent ATPase and a heat-stable coupling factor. 3. Other information obtained from reconstitution experiments include the role of asymmetry in organized membranes and the specificity of protein-phospholipid interaction. 4. Purified preparations of Ca++-ATPase catalyze the formation of ATP from Pi and ADP in a stepwise reaction stoichiometric with the enzyme and dependent on Ca++.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Bacteriorhodopsins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Carotenoids,
http://linkedlifedata.com/resource/pubmed/chemical/Ions,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium,
http://linkedlifedata.com/resource/pubmed/chemical/Protons,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0077-8923
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
264
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
17-33
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:130818-Adenosine Diphosphate,
pubmed-meshheading:130818-Adenosine Triphosphatases,
pubmed-meshheading:130818-Adenosine Triphosphate,
pubmed-meshheading:130818-Bacteriorhodopsins,
pubmed-meshheading:130818-Calcium,
pubmed-meshheading:130818-Carotenoids,
pubmed-meshheading:130818-Cell-Free System,
pubmed-meshheading:130818-Halobacterium,
pubmed-meshheading:130818-Hot Temperature,
pubmed-meshheading:130818-Ions,
pubmed-meshheading:130818-Light,
pubmed-meshheading:130818-Mitochondria,
pubmed-meshheading:130818-Models, Biological,
pubmed-meshheading:130818-Oxidative Phosphorylation,
pubmed-meshheading:130818-Phosphates,
pubmed-meshheading:130818-Phospholipids,
pubmed-meshheading:130818-Potassium,
pubmed-meshheading:130818-Protons,
pubmed-meshheading:130818-Sodium
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pubmed:year |
1975
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pubmed:articleTitle |
Resolution and reconstitution of ion-transport systems.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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