ArticleBiophysical journal2009
Ligand-dependent effects on the conformational equilibrium of the Na+,K+-ATPase as monitored by voltage clamp fluorometry.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- External Ion Access in the Na/K Pump: Kinetics of NaBiophysical journal · 2018Article
- Voltage Clamp Fluorometry of P-Type ATPases.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Examining the conformational dynamics of membrane proteins in situ with site-directed fluorescence labeling.Journal of visualized experiments : JoVE · 2011Article
- Identification of a potential receptor that couples ion transport to protein kinase activity.The Journal of biological chemistry · 2011Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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 E(1)/E(1)P. Furthermore, the K(+)(o)-induced relocation toward E(1) 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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