| pubmed-article:1832836 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1832836 | lifeskim:mentions | umls-concept:C2239176 | lld:lifeskim |
| pubmed-article:1832836 | lifeskim:mentions | umls-concept:C0026237 | lld:lifeskim |
| pubmed-article:1832836 | lifeskim:mentions | umls-concept:C1510699 | lld:lifeskim |
| pubmed-article:1832836 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:1832836 | lifeskim:mentions | umls-concept:C1553660 | lld:lifeskim |
| pubmed-article:1832836 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1832836 | pubmed:dateCreated | 1991-10-24 | lld:pubmed |
| pubmed-article:1832836 | pubmed:abstractText | A decrease in the rate of ATP hydrolysis was observed after preincubation of intact mitochondria from hepatoma 22a with an uncoupler. This effect is due both to a decrease in the rate of ATP transport and to an inactivation of the F0F1-ATPase. The former effect is shown to result from an uncoupler-induced ADP efflux. In de-energized mitochondria from hepatoma (but not from mice liver), the concentration of adenine nucleotides in the matrix equilibrates with the medium concentration via a carboxyatractyloside (CATR)-insensitive transport system. CATR-insensitive accumulation of medium ADP and stoichiometric exchange of added ATP are observed in energized hepatoma mitochondria. The dependence of the uncoupler-induced inactivation of ATPase activity on delta mu H+, pH, and ATP is consistent with the effect being caused by the natural protein inhibitor (IF1) of F0F1. ATP- and pH-dependent inactivation of the enzyme is also observed after disruption of mitochondria with the detergent Lubrol-WX. Almost all F0F1 in hepatoma mitochondria have IF1 bound in a noninhibitory manner. In the presence of uncoupler, this complex converts, via a reversible pH-dependent and an irreversible ATP-dependent process, to an inhibitory complex. The pH-dependent step can be blocked by Zn2+ and Cd2+ ions which probably bind to negatively charged residues on IF1, thereby preventing their protonation and conversion of the protein to an inhibitory conformation. | lld:pubmed |
| pubmed-article:1832836 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1832836 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1832836 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1832836 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1832836 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1832836 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1832836 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1832836 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1832836 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1832836 | pubmed:month | May | lld:pubmed |
| pubmed-article:1832836 | pubmed:issn | 0003-9861 | lld:pubmed |
| pubmed-article:1832836 | pubmed:author | pubmed-author:ChernyakB VBV | lld:pubmed |
| pubmed-article:1832836 | pubmed:author | pubmed-author:DukhovichV... | lld:pubmed |
| pubmed-article:1832836 | pubmed:author | pubmed-author:Khodjaev EYu | lld:pubmed |
| pubmed-article:1832836 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1832836 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:1832836 | pubmed:volume | 286 | lld:pubmed |
| pubmed-article:1832836 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1832836 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1832836 | pubmed:pagination | 604-9 | lld:pubmed |
| pubmed-article:1832836 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1832836 | pubmed:meshHeading | pubmed-meshheading:1832836-... | lld:pubmed |
| pubmed-article:1832836 | pubmed:meshHeading | pubmed-meshheading:1832836-... | lld:pubmed |
| pubmed-article:1832836 | pubmed:meshHeading | pubmed-meshheading:1832836-... | lld:pubmed |
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| pubmed-article:1832836 | pubmed:meshHeading | pubmed-meshheading:1832836-... | lld:pubmed |
| pubmed-article:1832836 | pubmed:meshHeading | pubmed-meshheading:1832836-... | lld:pubmed |
| pubmed-article:1832836 | pubmed:meshHeading | pubmed-meshheading:1832836-... | lld:pubmed |
| pubmed-article:1832836 | pubmed:meshHeading | pubmed-meshheading:1832836-... | lld:pubmed |
| pubmed-article:1832836 | pubmed:meshHeading | pubmed-meshheading:1832836-... | lld:pubmed |
| pubmed-article:1832836 | pubmed:meshHeading | pubmed-meshheading:1832836-... | lld:pubmed |
| pubmed-article:1832836 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1832836 | pubmed:articleTitle | Regulation of ATP hydrolysis in hepatoma 22a mitochondria. | lld:pubmed |
| pubmed-article:1832836 | pubmed:affiliation | A. N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR. | lld:pubmed |
| pubmed-article:1832836 | pubmed:publicationType | Journal Article | lld:pubmed |
