Article ID: CBB428130959

Finding Na,K-ATPase: I - From Cell to Molecule (2018)

unapi

The oppositely oriented concentration gradients of Na+ and K+ ions across the cell membrane as found in animal cells led to the requirement of an active ion-transport mechanism that maintains this steady-state condition. As solution of this problem the Na,K-ATPase was identified, a member of the P-type ATPase family. Its stoichiometry has been defined as 3 Na+/2 K+/1 ATP, and a class of Na,K-ATPase-specific inhibitors, cardiac steroids, was established, which allow the identification of this ion pump. In an effort lasting for several decades structural details were uncovered down to almost atomic resolution. The quaternary structure of the functional unit, either αβ heterodimer or (αβ)n complexes with n ≥ 2, is still under discussion.

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Citation URI
https://data.isiscb.org/isis/citation/CBB428130959/

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Authors & Contributors
Brockwell, John
Bungener, Patrick
Buscaglia, Marino L.
Day, David
Deichmann, Ute
Fantini, Bernardino
Journals
Journal of the History of Biology
Studies in History and Philosophy of Science Part C: Studies in History and Philosophy of Biological and Biomedical Sciences
Substantia: An International Journal of the History of Chemistry
Comptes Rendus Biologies
Endeavour: Review of the Progress of Science
Historical Records of Australian Science
Publishers
Armando
Brepols
Donzelli
Princeton University Press
University of Chicago Press
L'Asino d'oro Edizioni
Concepts
Biology
Biochemistry
Cytology
Microbiology
Genetics
Physiology
People
Beijerinck, Martinus Willem
Bergersen, Fraser John
Brachet, Jean
Dalcq, Albert
Darlington, Cyril Dean
Darwin, Charles Robert
Time Periods
20th century
21st century
19th century
20th century, early
20th century, late
Places
Australia
Europe
Italy
Spain
United States
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