| pubmed-article:6147134 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6147134 | lifeskim:mentions | umls-concept:C0036226 | lld:lifeskim |
| pubmed-article:6147134 | lifeskim:mentions | umls-concept:C0001477 | lld:lifeskim |
| pubmed-article:6147134 | lifeskim:mentions | umls-concept:C0042305 | lld:lifeskim |
| pubmed-article:6147134 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:6147134 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:6147134 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:6147134 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:6147134 | pubmed:dateCreated | 1984-9-17 | lld:pubmed |
| pubmed-article:6147134 | pubmed:abstractText | Ca2+ + Mg2+-dependent ATPase from sarcoplasmic reticulum was inhibited by preincubation with vanadate. When the inhibited enzyme was preincubated in the presence of vanadate and assayed in its absence, a slow reactivation process was observed. This slow, hysteretic, process was exploited to study the influence of Ca2+ and ATP on the dissociation of vanadate. Ca2+ alone slowly displaced vanadate from the inhibited enzyme, and a rate constant of 0.1 min-1, at 25 degrees C, was calculated for this re-activation process. However, ATP re-activated with an apparent constant that hyperbolically depended on ATP concentration, and from it a rate constant for vanadate dissociation induced by ATP of 0.5 min-1 was calculated. It is deduced from the kinetic studies that ATP binds to the enzyme-vanadate complex, forming a ternary complex, with a dissociation constant of 4 microM, and that this binding accelerates vanadate dissociation. Binding experiments with [14C]ATP showed that ATP binds to the enzyme-vanadate complex with a dissociation constant of 12 microM, i.e. the affinities calculated with the isotope technique and the kinetic procedure are of the same order of magnitude. | lld:pubmed |
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| pubmed-article:6147134 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6147134 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6147134 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6147134 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6147134 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:6147134 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:6147134 | pubmed:author | pubmed-author:García-Cánova... | lld:pubmed |
| pubmed-article:6147134 | pubmed:author | pubmed-author:García-Carmon... | lld:pubmed |
| pubmed-article:6147134 | pubmed:author | pubmed-author:Gómez-Fernánd... | lld:pubmed |
| pubmed-article:6147134 | pubmed:author | pubmed-author:OrtizAA | lld:pubmed |
| pubmed-article:6147134 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6147134 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:6147134 | pubmed:volume | 221 | lld:pubmed |
| pubmed-article:6147134 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6147134 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6147134 | pubmed:pagination | 213-22 | lld:pubmed |
| pubmed-article:6147134 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:6147134 | pubmed:meshHeading | pubmed-meshheading:6147134-... | lld:pubmed |
| pubmed-article:6147134 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6147134 | pubmed:articleTitle | A kinetic study of the interaction of vanadate with the Ca2+ + Mg2+-dependent ATPase from sarcoplasmic reticulum. | lld:pubmed |
| pubmed-article:6147134 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6147134 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
