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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1989-7-25
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pubmed:abstractText |
A method is described for studying the coupling ratio of the Na+/K+ pump, i.e., the ratio of pump-mediated fluxes of Na+ and K+, in a reconstituted system. The method is based on the comparison of the pump-generated current with the rate of K+ transport. Na+/K+-ATPase from kidney is incorporated into the membrane of artificial lipid vesicles; ATPase molecules with outward-oriented ATP-binding site are activated by addition of ATP to the medium. Using oxonol VI as a potential-sensitive dye for measuring transmembrane voltage, the pump current is determined from the change of voltage with time t. In a second set of experiments, the membrane is made selectively K+-permeable by addition of valinomycin, so that the membrane voltage U is equal to the Nernst potential of K+. Under this condition, dU/dt reflects the change of intravesicular K+ concentration and thus the flux of K+. Values of the Na+/K+ coupling ratio determined in this way are close to 1.5 in the experimental range (10-75 mM) of extravesicular (cytoplasmic) Na+ concentrations.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Isoxazoles,
http://linkedlifedata.com/resource/pubmed/chemical/Liposomes,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Potassium-Exchanging ATPase,
http://linkedlifedata.com/resource/pubmed/chemical/oxonol VI
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
981
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
326-36
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2543461-Animals,
pubmed-meshheading:2543461-Biological Transport, Active,
pubmed-meshheading:2543461-Isoxazoles,
pubmed-meshheading:2543461-Kidney Medulla,
pubmed-meshheading:2543461-Kinetics,
pubmed-meshheading:2543461-Liposomes,
pubmed-meshheading:2543461-Membrane Lipids,
pubmed-meshheading:2543461-Membrane Potentials,
pubmed-meshheading:2543461-Potassium,
pubmed-meshheading:2543461-Rabbits,
pubmed-meshheading:2543461-Sodium,
pubmed-meshheading:2543461-Sodium-Potassium-Exchanging ATPase,
pubmed-meshheading:2543461-Spectrometry, Fluorescence,
pubmed-meshheading:2543461-Thermodynamics
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pubmed:year |
1989
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pubmed:articleTitle |
Pump current and Na+/K+ coupling ratio of Na+/K+-ATPase in reconstituted lipid vesicles.
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pubmed:affiliation |
Department of Biology, University of Konstanz, F.R.G.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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