pubmed-article:17766357 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17766357 | lifeskim:mentions | umls-concept:C0001479 | lld:lifeskim |
pubmed-article:17766357 | lifeskim:mentions | umls-concept:C1706470 | lld:lifeskim |
pubmed-article:17766357 | lifeskim:mentions | umls-concept:C1706469 | lld:lifeskim |
pubmed-article:17766357 | pubmed:issue | 12 | lld:pubmed |
pubmed-article:17766357 | pubmed:dateCreated | 2007-11-29 | lld:pubmed |
pubmed-article:17766357 | pubmed:abstractText | The kinetics of the phosphorylation and subsequent conformational change of Na(+),K(+)-ATPase was investigated via the stopped-flow technique using the fluorescent label RH421 (pH 7.4, 24 degrees C). The enzyme was preequilibrated in buffer containing 130 mM NaCl to stabilize the E1(Na(+))(3) state. On mixing with ATP in the presence of Mg(2+), a fluorescence increase occurred, due to enzyme conversion into the E2P state. The fluorescence change accelerated with increasing ATP concentration until a saturating limit in the hundreds of micromolar range. The amplitude of the fluorescence change (DeltaF/F(0)) increased to 0.98 at 50 microM ATP. DeltaF/F(0) then decreased to 0.82 at 500 microM. The decrease was attributed to an ATP-induced allosteric acceleration of the dephosphorylation reaction. The ATP concentration dependence of the time course and the amplitude of the fluorescence change could not be explained by either a one-site monomeric enzyme model or by a two-pool model. All of the data could be explained by an (alphabeta)(2) dimeric model, in which the enzyme cycles at a low rate with ATP hydrolysis by one alpha-subunit or at a high rate with ATP hydrolysis by both alpha-subunits. Thus, we propose a two-gear bicyclic model to replace the classical monomeric Albers-Post model for kidney Na(+),K(+)-ATPase. | lld:pubmed |
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pubmed-article:17766357 | pubmed:language | eng | lld:pubmed |
pubmed-article:17766357 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17766357 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17766357 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17766357 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17766357 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17766357 | pubmed:month | Dec | lld:pubmed |
pubmed-article:17766357 | pubmed:issn | 1542-0086 | lld:pubmed |
pubmed-article:17766357 | pubmed:author | pubmed-author:ClarkeRonald... | lld:pubmed |
pubmed-article:17766357 | pubmed:author | pubmed-author:KaneDavid JDJ | lld:pubmed |
pubmed-article:17766357 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:17766357 | pubmed:day | 15 | lld:pubmed |
pubmed-article:17766357 | pubmed:volume | 93 | lld:pubmed |
pubmed-article:17766357 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17766357 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17766357 | pubmed:pagination | 4187-96 | lld:pubmed |
pubmed-article:17766357 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:17766357 | pubmed:meshHeading | pubmed-meshheading:17766357... | lld:pubmed |
pubmed-article:17766357 | pubmed:meshHeading | pubmed-meshheading:17766357... | lld:pubmed |
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pubmed-article:17766357 | pubmed:meshHeading | pubmed-meshheading:17766357... | lld:pubmed |
pubmed-article:17766357 | pubmed:meshHeading | pubmed-meshheading:17766357... | lld:pubmed |
pubmed-article:17766357 | pubmed:meshHeading | pubmed-meshheading:17766357... | lld:pubmed |
pubmed-article:17766357 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17766357 | pubmed:articleTitle | Two gears of pumping by the sodium pump. | lld:pubmed |
pubmed-article:17766357 | pubmed:affiliation | School of Chemistry, University of Sydney, Sydney, Australia. r.clarke@chem.usyd.edu.au | lld:pubmed |
pubmed-article:17766357 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17766357 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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