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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Authors & Contributors
Santesmases, María Jesús
Henry, Marc
Adriana Giannini
Fabrizio Rufo
Fasolo, Aldo
Passariello, Alessandra
Journals
Substantia: An International Journal of the History of Chemistry
Studies in History and Philosophy of Science Part C: Studies in History and Philosophy of Biological and Biomedical Sciences
Journal of the History of Biology
Medicina Historica
Mefisto: Rivista di medicina, filosofia, storia
Perspectives in Biology and Medicine
Publishers
Armando
L'Asino d'oro Edizioni
University of Chicago Press
Princeton University Press
Donzelli
Brepols
Concepts
Biology
Biochemistry
Cytology
Microbiology
Genetics
Physiology
People
Rheinberger, Hans-Jörg
Margulis, Lynn
Levi-Montalcini, Rita
Levan, Albert
Kühn, Alfred
Kluyver, Albert Jan
Time Periods
20th century
21st century
19th century
20th century, early
20th century, late
Places
United States
Spain
Italy
Europe
Australia
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