| pubmed-article:19413981 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19413981 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:19413981 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:19413981 | lifeskim:mentions | umls-concept:C0597484 | lld:lifeskim |
| pubmed-article:19413981 | lifeskim:mentions | umls-concept:C2346927 | lld:lifeskim |
| pubmed-article:19413981 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:19413981 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:19413981 | pubmed:dateCreated | 2009-5-5 | lld:pubmed |
| pubmed-article:19413981 | pubmed:abstractText | The Mg(2+) dependence of the kinetics of the phosphorylation and conformational changes of Na(+),K(+)-ATPase was investigated via the stopped-flow technique using the fluorescent label RH421. The enzyme was preequilibrated in buffer containing 130 mM NaCl to stabilize the E1(Na(+))(3) state. On mixing with ATP, a fluorescence increase was observed. Two exponential functions were necessary to fit the data. Both phases displayed an increase in their observed rate constants with increasing Mg(2+) to saturating values of 195 (+/- 6) s(-1) and 54 (+/- 8) s(-1) for the fast and slow phases, respectively. The fast phase was attributed to enzyme conversion into the E2MgP state. The slow phase was attributed to relaxation of the dephosphorylation/rephosphorylation (by ATP) equilibrium and the buildup of some enzyme in the E2Mg state. Taking into account competition from free ATP, the dissociation constant (K(d)) of Mg(2+) interaction with the E1ATP(Na(+))(3) state was estimated as 0.069 (+/- 0.010) mM. This is virtually identical to the estimated value of the K(d) of Mg(2+)-ATP interaction in solution. Within the enzyme-ATP-Mg(2+) complex, the actual K(d) for Mg(2+) binding can be attributed primarily to complexation by ATP itself, with no apparent contribution from coordination by residues of the enzyme environment in the E1 conformation. | lld:pubmed |
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| pubmed-article:19413981 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19413981 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19413981 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19413981 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19413981 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19413981 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19413981 | pubmed:month | May | lld:pubmed |
| pubmed-article:19413981 | pubmed:issn | 1542-0086 | lld:pubmed |
| pubmed-article:19413981 | pubmed:author | pubmed-author:SebbanPierreP | lld:pubmed |
| pubmed-article:19413981 | pubmed:author | pubmed-author:CorneliusFlem... | lld:pubmed |
| pubmed-article:19413981 | pubmed:author | pubmed-author:ClarkeRonald... | lld:pubmed |
| pubmed-article:19413981 | pubmed:author | pubmed-author:KuchelPhilip... | lld:pubmed |
| pubmed-article:19413981 | pubmed:author | pubmed-author:Pilotelle-Bun... | lld:pubmed |
| pubmed-article:19413981 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19413981 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:19413981 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:19413981 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19413981 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19413981 | pubmed:pagination | 3753-61 | lld:pubmed |
| pubmed-article:19413981 | pubmed:dateRevised | 2010-9-27 | lld:pubmed |
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| pubmed-article:19413981 | pubmed:meshHeading | pubmed-meshheading:19413981... | lld:pubmed |
| pubmed-article:19413981 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19413981 | pubmed:articleTitle | Mechanism of Mg2+ binding in the Na+,K+-ATPase. | lld:pubmed |
| pubmed-article:19413981 | pubmed:affiliation | School of Chemistry, University of Sydney, Sydney, New South Wales, Australia. | lld:pubmed |
| pubmed-article:19413981 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19413981 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
