| pubmed-article:2526696 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2526696 | lifeskim:mentions | umls-concept:C0205474 | lld:lifeskim |
| pubmed-article:2526696 | lifeskim:mentions | umls-concept:C1135183 | lld:lifeskim |
| pubmed-article:2526696 | lifeskim:mentions | umls-concept:C0018787 | lld:lifeskim |
| pubmed-article:2526696 | lifeskim:mentions | umls-concept:C0031603 | lld:lifeskim |
| pubmed-article:2526696 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
| pubmed-article:2526696 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:2526696 | lifeskim:mentions | umls-concept:C0205265 | lld:lifeskim |
| pubmed-article:2526696 | lifeskim:mentions | umls-concept:C1555582 | lld:lifeskim |
| pubmed-article:2526696 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2526696 | pubmed:dateCreated | 1989-8-31 | lld:pubmed |
| pubmed-article:2526696 | pubmed:abstractText | The actin dependence of the rate and magnitude of the initial phosphate burst was measured using both quench-flow and stopped-flow kinetic techniques. These studies revealed that even at high actin concentrations the magnitude of the phosphate burst was a significant fraction of the magnitude that exists in the absence of actin. Furthermore, it was shown that the rate of the burst rises rapidly as a function of the actin concentration. Detailed modeling with the four-state model revealed that if the predicted Vmax is constrained to be approximately equal to the extrapolated value (double reciprocal plot) and if the apparent dissociation constant of subfragment-1 to actin divided by the apparent activation constant of the actin-activated myosin ATPase activity (Kbinding/KATPase) is constrained to be considerably different from one, then the model is unable to simultaneously account for the ATPase activity and the rate and magnitude of the initial inorganic phosphate burst. | lld:pubmed |
| pubmed-article:2526696 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2526696 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2526696 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2526696 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2526696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2526696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2526696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2526696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2526696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2526696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2526696 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2526696 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2526696 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:2526696 | pubmed:issn | 0009-7330 | lld:pubmed |
| pubmed-article:2526696 | pubmed:author | pubmed-author:SteinL ALA | lld:pubmed |
| pubmed-article:2526696 | pubmed:author | pubmed-author:WhiteM PMP | lld:pubmed |
| pubmed-article:2526696 | pubmed:author | pubmed-author:AnnisD TDT | lld:pubmed |
| pubmed-article:2526696 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2526696 | pubmed:volume | 65 | lld:pubmed |
| pubmed-article:2526696 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2526696 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2526696 | pubmed:pagination | 515-25 | lld:pubmed |
| pubmed-article:2526696 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:2526696 | pubmed:meshHeading | pubmed-meshheading:2526696-... | lld:pubmed |
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| pubmed-article:2526696 | pubmed:meshHeading | pubmed-meshheading:2526696-... | lld:pubmed |
| pubmed-article:2526696 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2526696 | pubmed:articleTitle | Biochemical kinetics of porcine cardiac subfragment-1. II. Pre-steady-state studies of the initial phosphate burst. | lld:pubmed |
| pubmed-article:2526696 | pubmed:affiliation | Department of Medicine, State University of New York, Stony Brook 11794. | lld:pubmed |
| pubmed-article:2526696 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2526696 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2526696 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2526696 | lld:pubmed |
