| pubmed-article:6239651 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6239651 | lifeskim:mentions | umls-concept:C0006675 | lld:lifeskim |
| pubmed-article:6239651 | lifeskim:mentions | umls-concept:C0001476 | lld:lifeskim |
| pubmed-article:6239651 | lifeskim:mentions | umls-concept:C0001480 | lld:lifeskim |
| pubmed-article:6239651 | lifeskim:mentions | umls-concept:C0205681 | lld:lifeskim |
| pubmed-article:6239651 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:6239651 | pubmed:issue | 23 | lld:pubmed |
| pubmed-article:6239651 | pubmed:dateCreated | 1985-1-31 | lld:pubmed |
| pubmed-article:6239651 | pubmed:abstractText | The complex of Mg X ATP and the calcium adenosinetriphosphatase of sarcoplasmic reticulum (E X ATP) reacts with 50-300 microM Ca2+ to form phosphoenzyme (E-P X Ca2) with a rate constant of 70 s-1 (pH 7.0, 100 mM KCl, 5 mM MgSO4, 25 degrees C, and SR vesicles passively loaded with Ca2+). This rate constant is independent of Ca2+ concentration above 50 microM. It is 4-6 times faster than the rate constants of 11-15 s-1 for the conformational change associated with Ca2+ binding in the absence of activation by ATP. The reaction of 200 microM Ca2+ with enzyme preincubated in 0.9 microM [gamma-32P]ATP X Mg shows a burst of [32P]E-P X Ca2 formation. This result indicates that Mg X ATP bound to the active site, and not a regulatory site, can accelerate the conformational change associated with Ca2+ binding because this concentration of Mg X ATP is well below the Kd of 160-500 microM for the putative regulatory site. When an unlabeled ATP chase is added with the Ca2+ to enzyme preincubated with [gamma-32P]ATP X Mg, the amount of [32P]E-P X Ca2 that is formed increases with the concentration of ATP in the preincubation solution and is consistent with a maximum fraction trapped of 0.55 and Kd = 4.5 microM for the dissociation of Mg X ATP from the active site. The fact that labeled E X ATP can be trapped by added Ca2+ confirms the conclusion that dissociation of ATP from E X ATP X Ca2 is slow relative to phosphorylation. | lld:pubmed |
| pubmed-article:6239651 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6239651 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6239651 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6239651 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6239651 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6239651 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6239651 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6239651 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6239651 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:6239651 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:6239651 | pubmed:author | pubmed-author:JencksW PWP | lld:pubmed |
| pubmed-article:6239651 | pubmed:author | pubmed-author:StahlNN | lld:pubmed |
| pubmed-article:6239651 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6239651 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:6239651 | pubmed:volume | 23 | lld:pubmed |
| pubmed-article:6239651 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6239651 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6239651 | pubmed:pagination | 5389-92 | lld:pubmed |
| pubmed-article:6239651 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:6239651 | pubmed:meshHeading | pubmed-meshheading:6239651-... | lld:pubmed |
| pubmed-article:6239651 | pubmed:meshHeading | pubmed-meshheading:6239651-... | lld:pubmed |
| pubmed-article:6239651 | pubmed:meshHeading | pubmed-meshheading:6239651-... | lld:pubmed |
| pubmed-article:6239651 | pubmed:meshHeading | pubmed-meshheading:6239651-... | lld:pubmed |
| pubmed-article:6239651 | pubmed:meshHeading | pubmed-meshheading:6239651-... | lld:pubmed |
| pubmed-article:6239651 | pubmed:meshHeading | pubmed-meshheading:6239651-... | lld:pubmed |
| pubmed-article:6239651 | pubmed:meshHeading | pubmed-meshheading:6239651-... | lld:pubmed |
| pubmed-article:6239651 | pubmed:meshHeading | pubmed-meshheading:6239651-... | lld:pubmed |
| pubmed-article:6239651 | pubmed:meshHeading | pubmed-meshheading:6239651-... | lld:pubmed |
| pubmed-article:6239651 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6239651 | pubmed:articleTitle | Adenosine 5'-triphosphate at the active site accelerates binding of calcium to calcium adenosinetriphosphatase. | lld:pubmed |
| pubmed-article:6239651 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6239651 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6239651 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6239651 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6239651 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6239651 | lld:pubmed |
