| pubmed-article:10388756 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10388756 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:10388756 | lifeskim:mentions | umls-concept:C0003075 | lld:lifeskim |
| pubmed-article:10388756 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:10388756 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:10388756 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
| pubmed-article:10388756 | lifeskim:mentions | umls-concept:C0597484 | lld:lifeskim |
| pubmed-article:10388756 | lifeskim:mentions | umls-concept:C0728938 | lld:lifeskim |
| pubmed-article:10388756 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10388756 | pubmed:dateCreated | 1999-7-30 | lld:pubmed |
| pubmed-article:10388756 | pubmed:abstractText | The effects of lyotropic anions, particularly perchlorate, on the kinetics of partial reactions of the Na+,K+-ATPase from pig kidney were investigated by two different kinetic techniques: stopped flow in combination with the fluorescent label RH421 and a stationary electrical relaxation technique. It was found that 130 mM NaClO4 caused an increase in the Kd values of both the high- and low-affinity ATP-binding sites, from values of 7.0 (+/- 0.6) microM and 143 (+/- 17) microM in 130 mM NaCl solution to values of 42 (+/- 3) microM and 660 (+/- 100) microM in 130 mM NaClO4 (pH 7.4, 24 degrees C). The half-saturating concentration of the Na+-binding sites on the E1 conformation was found to decrease from 8-10 mM in NaCl to 2.5-3.5 mM in NaClO4 solution. The rate of equilibration of the reaction, E1P(Na+)3 left arrow over right arrow E2P + 3Na+, decreased from 393 (+/- 51) s-1 in NaCl solution to 114 (+/- 15) s-1 in NaClO4. This decrease is attributed predominantly to an inhibition of the E1P(Na+)3 --> E2P(Na+)3 transition. The effects can be explained in terms of electrostatic interactions due to perchlorate binding within the membrane and/or protein matrix of the Na+,K+-ATPase membrane fragments and alteration of the local electric field strength experienced by the protein. The kinetic results obtained support the conclusion that the conformational transition E1P(Na+)3 --> E2P(Na+)3 is a major charge translocating step of the pump cycle. | lld:pubmed |
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| pubmed-article:10388756 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10388756 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10388756 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10388756 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10388756 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10388756 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:10388756 | pubmed:author | pubmed-author:FendlerKK | lld:pubmed |
| pubmed-article:10388756 | pubmed:author | pubmed-author:GrellEE | lld:pubmed |
| pubmed-article:10388756 | pubmed:author | pubmed-author:GaneaCC | lld:pubmed |
| pubmed-article:10388756 | pubmed:author | pubmed-author:ClarkeR JRJ | lld:pubmed |
| pubmed-article:10388756 | pubmed:author | pubmed-author:BabesAA | lld:pubmed |
| pubmed-article:10388756 | pubmed:author | pubmed-author:LüpfertCC | lld:pubmed |
| pubmed-article:10388756 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10388756 | pubmed:volume | 77 | lld:pubmed |
| pubmed-article:10388756 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10388756 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10388756 | pubmed:pagination | 267-81 | lld:pubmed |
| pubmed-article:10388756 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:10388756 | pubmed:meshHeading | pubmed-meshheading:10388756... | lld:pubmed |
| pubmed-article:10388756 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10388756 | pubmed:articleTitle | Hofmeister effects of anions on the kinetics of partial reactions of the Na+,K+-ATPase. | lld:pubmed |
| pubmed-article:10388756 | pubmed:affiliation | Department of Biophysics, C. Davila Medical University, 76241 Bucharest, Romania. | lld:pubmed |
| pubmed-article:10388756 | pubmed:publicationType | Journal Article | lld:pubmed |
