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PMID: 1328174 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

The Na,K-ATPase.

Journal of bioenergetics and biomembranes ·Vol. 24 ·No. 3 ·1992-06-00 ·Pages 249-61

Skou JC, Esmann M

Abstract

The energy dependent exchange of cytoplasmic Na+ for extracellular K+ in mammalian cells is due to a membrane bound enzyme system, the Na,K-ATPase. The exchange sustains a gradient for Na+ into and for K+ out of the cell, and this is used as an energy source for creation of the membrane potential, for its de- and repolarisation, for regulation of cytoplasmic ionic composition and for transepithelial transport. The Na,K-ATPase consists of two membrane spanning polypeptides, an alpha-subunit of 112-kD and a beta-subunit, which is a glycoprotein of 35-kD. The catalytic properties are associated with the alpha-subunit, which has the binding domain for ATP and the cations. In the review, attention will be given to the biochemical characterization of the reaction mechanism underlying the coupling between hydrolysis of the substate ATP and transport of Na+ and K+.

MeSH Terms
Adenosine Triphosphate/metabolism Animals Binding Sites Cell Membrane/enzymology Potassium/metabolism Protein Conformation Sodium/metabolism Sodium-Potassium-Exchanging ATPase/antagonists & inhibitors,chemistry,metabolism
Chemicals
Adenosine Triphosphate Sodium Sodium-Potassium-Exchanging ATPase Potassium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Skou J C
Institute of Biophysics, University of Aarhus, Denmark.
Esmann M
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Article Info
Journal
Journal of bioenergetics and biomembranes
Abbr.
J Bioenerg Biomembr
ISSN
0145-479X
DOI
10.1007/BF00768846
Published
1992-06-00
Pages
249-61
Language
English
Region
United States
NLM ID
7701859
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00768846 View journal details
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