| pubmed-article:6223627 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6223627 | lifeskim:mentions | umls-concept:C0521451 | lld:lifeskim |
| pubmed-article:6223627 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:6223627 | lifeskim:mentions | umls-concept:C0001506 | lld:lifeskim |
| pubmed-article:6223627 | lifeskim:mentions | umls-concept:C0018366 | lld:lifeskim |
| pubmed-article:6223627 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:6223627 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:6223627 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:6223627 | pubmed:dateCreated | 1983-8-11 | lld:pubmed |
| pubmed-article:6223627 | pubmed:abstractText | 1. The presence of 5'-adenylyl imidodiphosphate, a non-hydrolysable analogue of ATP, in the solution used to assay the soluble bovine heart mitochondrial F1-ATPase produced slow competitive inhibition. If the enzyme was preincubated with the inhibitor before the substrate, MgATP, was added, a partial re-activation was obtained. 2. The slow inhibitory process showed first-order rate kinetics, and therefore it seems likely that a conformational change of the enzyme occurs following a faster binding process. A reaction scheme is suggested. At pH 7.8 the rate constant for the inhibition reaction was calculated to be 6.7 X 10(-2)s-1 and that for the re-activation 3.8 X 10(-3)s-1, with Keq. 17.6, indicating that the inhibited enzyme-inhibitor complex will be favoured over the non-inhibited enzyme-inhibitor complex. 3. The presence of 5'-guanylyl imidodiphosphate in the solution used to assay F1-ATPase produced rapid competitive inhibition, which was then slowly reversed until a steady state was reached. This might be explained by a rapid but reversible shift of the inhibition pathway induced by this non-hydrolysable analogue of ATP. A complex rate constant for the displacement of the inhibitor by the substrate of 7.6 X 10(-3)s-1 was calculated. 4. The results are discussed in the light of other recent observations about binding of 5'-adenylyl imidodiphosphate to F1-ATPase and with reference to the binding-site-change mechanism of hydrolysis of ATP by F1-ATPase. | lld:pubmed |
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| pubmed-article:6223627 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6223627 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6223627 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6223627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:6223627 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6223627 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:6223627 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:6223627 | pubmed:author | pubmed-author:LozanoJ AJA | lld:pubmed |
| pubmed-article:6223627 | pubmed:author | pubmed-author:CarmonaF GFG | lld:pubmed |
| pubmed-article:6223627 | pubmed:author | pubmed-author:CánovasF GFG | lld:pubmed |
| pubmed-article:6223627 | pubmed:author | pubmed-author:Gómez-Fernánd... | lld:pubmed |
| pubmed-article:6223627 | pubmed:author | pubmed-author:BeldaF JFJ | lld:pubmed |
| pubmed-article:6223627 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6223627 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:6223627 | pubmed:volume | 210 | lld:pubmed |
| pubmed-article:6223627 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6223627 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6223627 | pubmed:pagination | 727-35 | lld:pubmed |
| pubmed-article:6223627 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:6223627 | pubmed:meshHeading | pubmed-meshheading:6223627-... | lld:pubmed |
| pubmed-article:6223627 | pubmed:meshHeading | pubmed-meshheading:6223627-... | lld:pubmed |
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| pubmed-article:6223627 | pubmed:meshHeading | pubmed-meshheading:6223627-... | lld:pubmed |
| pubmed-article:6223627 | pubmed:year | 1983 | lld:pubmed |
| pubmed-article:6223627 | pubmed:articleTitle | A kinetic study of the interaction between mitochondrial F1 adenosine triphosphatase and adenylyl imidodiphosphate and guanylyl imidodiphosphate. | lld:pubmed |
| pubmed-article:6223627 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6223627 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6223627 | lld:pubmed |
