| pubmed-article:6451621 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6451621 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:6451621 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:6451621 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:6451621 | lifeskim:mentions | umls-concept:C0439857 | lld:lifeskim |
| pubmed-article:6451621 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:6451621 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:6451621 | lifeskim:mentions | umls-concept:C1554963 | lld:lifeskim |
| pubmed-article:6451621 | lifeskim:mentions | umls-concept:C0457405 | lld:lifeskim |
| pubmed-article:6451621 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:6451621 | pubmed:dateCreated | 1981-5-26 | lld:pubmed |
| pubmed-article:6451621 | pubmed:abstractText | A convenient and reliable method to measure passive H+-translocating activity (H+ conductivity) was developed; vesicles reconstituted from the membrane moiety (F0) of H+-ATPase (F0 . F1) and soybean phospholipids were loaded with KCl by a freeze-thaw-sonication procedure and the rate of H+ uptake caused by the K+ diffusion potential upon addition of valinomycin was followed with a pH meter. Of the methods tested, a dialysis method using cholate plus deoxycholate gave the best results for reconstitution. Using this method, H+ conductivity of the membrane moiety of H+-ATPase from a thermophilic bacterium PS3 (TF0) was analyzed. Dependence of H+ conductivity of TF0 on H+ concentration fitted a Michaelis-Menten equation showing a Vmax of 31.3 microgram ion/min . mg of TF0 and a Km of 0.095 microgram ion/liter. Upon modification of a tyrosyl residue of TF0 with iodine, the Km value shifted to 0.71 microgram ion/liter, while the Vmax remained constant. These results were interpreted as indicating that a single tyrosyl residue in N,N'-dicyclohexylcarbodiimide-binding proteolipid of TF0 plays an important role as an H+ donor in the the rate-limiting step of H+ permeation through TF0. TF1, the catalytic moiety of H+-ATPase from the thermophilic bacterium PS3, blocked H+ conduction through TF0. A 1:1 stoichiometry of TF1 and TF0 was found in ATP-dependent membrane potential generation as well as H+ conduction. | lld:pubmed |
| pubmed-article:6451621 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6451621 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6451621 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6451621 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6451621 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6451621 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6451621 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6451621 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6451621 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6451621 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6451621 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:6451621 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:6451621 | pubmed:author | pubmed-author:KagawaYY | lld:pubmed |
| pubmed-article:6451621 | pubmed:author | pubmed-author:SoniJJ | lld:pubmed |
| pubmed-article:6451621 | pubmed:author | pubmed-author:HamamotoTT | lld:pubmed |
| pubmed-article:6451621 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6451621 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:6451621 | pubmed:volume | 256 | lld:pubmed |
| pubmed-article:6451621 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6451621 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6451621 | pubmed:pagination | 2873-7 | lld:pubmed |
| pubmed-article:6451621 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:6451621 | pubmed:meshHeading | pubmed-meshheading:6451621-... | lld:pubmed |
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| pubmed-article:6451621 | pubmed:meshHeading | pubmed-meshheading:6451621-... | lld:pubmed |
| pubmed-article:6451621 | pubmed:meshHeading | pubmed-meshheading:6451621-... | lld:pubmed |
| pubmed-article:6451621 | pubmed:meshHeading | pubmed-meshheading:6451621-... | lld:pubmed |
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| pubmed-article:6451621 | pubmed:meshHeading | pubmed-meshheading:6451621-... | lld:pubmed |
| pubmed-article:6451621 | pubmed:year | 1981 | lld:pubmed |
| pubmed-article:6451621 | pubmed:articleTitle | pH dependence of H+ conduction through the membrane moiety of the H+-ATPase (F0 . F1) and effects of tyrosyl residue modification. | lld:pubmed |
| pubmed-article:6451621 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6451621 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6451621 | lld:pubmed |
