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  Ligand-Dependent Effects on the Conformational Equilibrium of the Na+,K+-ATPase As Monitored by Voltage Clamp Fluorometry

Geys, S., Bamberg, E., & Dempski, R. E. (2009). Ligand-Dependent Effects on the Conformational Equilibrium of the Na+,K+-ATPase As Monitored by Voltage Clamp Fluorometry. Biophysical Journal, 96(11), 4561-4570. doi:10.1016/j.bpj.2009.03.002.

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 Creators:
Geys, Stefan1, Author           
Bamberg, Ernst1, 2, Author           
Dempski, Robert E.1, Author           
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              
2Chemical and Pharmaceutical Sciences Department, Johann Wolfgang Goethe University Frankfurt, Frankfurt am Main, Germany, ou_persistent22              

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 Abstract: Voltage clamp fluorometry was used to monitor conformational changes associated with electrogenic partial reactions of the Na+,K+-ATPase after changes in the concentration of internal sodium (Na+i) or external potassium (K+o). To probe the effects of the Na+i concentration on the Na+ branch of the Na+,K+-ATPase, oocytes were depleted of Na+i and then loaded with external sodium (Na+o) using the amiloride-sensitive epithelial sodium channel. The K+ branch of the Na+,K+-ATPase was studied by exposing the oocytes to different K+o concentrations in the presence and absence of Na+o to obtain additional information on the apparent affinity for K+o. Our results demonstrate that lowering the concentration of Na+i or increasing the amount of K+o in the external solution shifts the equilibrium toward E1/E1P. Furthermore, the K+o-induced relocation toward E1 occurs at a much lower K+o concentration when Na+o is absent, indicating a higher apparent affinity. Finally, voltage-dependent steps associated with the K+ branch or the Na+ branch of the Na+,K+-ATPase are affected by the K+o concentration or the Na+i concentration, respectively.

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Language(s): eng - English
 Dates: 2008-10-142009-03-062009-06-03
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bpj.2009.03.002
PMID: 19486678
PMC: PMC2711450
 Degree: -

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Title: Biophysical Journal
  Other : Biophys. J.
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 96 (11) Sequence Number: - Start / End Page: 4561 - 4570 Identifier: ISSN: 0006-3495
CoNE: https://pure.mpg.de/cone/journals/resource/954925385117