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lifeskim:mentions |
umls-concept:C0013790,
umls-concept:C0029144,
umls-concept:C0040704,
umls-concept:C0040715,
umls-concept:C0182537,
umls-concept:C0392747,
umls-concept:C0442828,
umls-concept:C0599718,
umls-concept:C0599813,
umls-concept:C0599893,
umls-concept:C0687129,
umls-concept:C1522702,
umls-concept:C1705165,
umls-concept:C1707455,
umls-concept:C2700061
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pubmed:issue |
1
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pubmed:dateCreated |
1989-11-2
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pubmed:abstractText |
The electrogenic properties of the Na,K-ATPase were studied by correlating transient electrical events in the pump molecule with conformational transitions elicited by an ATP-concentration jump. Flat membrane fragments containing a high density (approximately 8000 microm(-2)) of oriented Na,K-ATPase molecules were bound to a planar lipid bilayer acting as a capacitive electrode. ATP was released in the medium from a photolabile inactive ATP derivative ("caged" ATP) by a 40-microsec light flash. Electrical signals resulting from transient charge movements in the protein under single-turnover conditions were recorded in the external measuring circuit. In parallel experiments carried out under virtually identical conditions, the fluorescence of membrane fragments containing Na,K-ATPase with covalently-bound 5-iodoacetamido-fluorescein (5-IAF) was monitored after the ATP-concentration jump. When the medium contained Na+, but no K+, the fluorescence of the 5-IAF-labeled protein decreases monotonously after release of ATP. In the experiments with membrane fragments bound to a planar bilayer, a transient pump current was observed which exhibited virtually the same time behavior as the fluorescence decay. This indicates that optical and electrical transients are governed by the same rate-limiting reaction step. Experiments with chymotrypsin-modified Na,K-ATPase suggest that both the fluorescence change as well as the charge movement are associated with the deocclusion of Na+ and release to the extracellular side. In experiments with Na+-free K+ media, a large inverse fluorescence change is observed after the ATP-concentration jump, but no charge translocation can be detected. This indicates that deocclusion of K+ is an electrically silent process.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0022-2631
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
110
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
67-86
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2552127-Animals,
pubmed-meshheading:2552127-Chymotrypsin,
pubmed-meshheading:2552127-Electricity,
pubmed-meshheading:2552127-Fluorescence,
pubmed-meshheading:2552127-Fluorescent Dyes,
pubmed-meshheading:2552127-Kidney Medulla,
pubmed-meshheading:2552127-Kinetics,
pubmed-meshheading:2552127-Rabbits,
pubmed-meshheading:2552127-Sodium-Potassium-Exchanging ATPase,
pubmed-meshheading:2552127-Statistics as Topic
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pubmed:year |
1989
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pubmed:articleTitle |
Conformational transitions and change translocation by the Na,K pump: comparison of optical and electrical transients elicited by ATP-concentration jumps.
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pubmed:affiliation |
Department of Biology, University of Konstanz, Federal Republic of Germany.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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