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The oligomeric nature of Na/K-transport ATPase
Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
2001 (English)In: Journal of Biochemistry (Tokyo), ISSN 0021-924X, E-ISSN 1756-2651, Vol. 129, no 3, 335-342 p.Article in journal (Refereed) Published
Abstract [en]

Since the discovery of Na/K-ATPase, evidence has accumulated to suggest that 1 mol of ATP hydrolysis occurs via the Na+-occluded ADP-sensitive phosphoenzyme, the K+-sensitive phosphoenzyme and the K+-occluded enzyme accompanying active transport of 3Na+ and 2K+ according the Post-Albers scheme. However, some controversial issues have arisen concerning whether the functional unit of the enzyme is an a▀-protomer or a much higher oligomer, which would be related to the mechanism of transport, either sequential or simultaneous. Detailed studies of oligomer interaction and the reactivity of the enzyme and a comparison of the extent of phosphorylation with ligand-binding capacities in the presence or absence of ATP hydrolysis and others strongly suggest that the functional unit of the enzyme in the membrane is a tetraprotomer, (a▀)4. They also suggest that each reaction intermediate of the Post-Albers scheme, respectively, reflects half of the site property of the intermediate and that another half binds ATP. These data may be useful not only to answer the long-standing question of whether the mechanism functions in the presence of both Na+ and K+ but also contribute to a better understanding of the mechanism of P-type pump ATPase in general.

Place, publisher, year, edition, pages
2001. Vol. 129, no 3, 335-342 p.
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:liu:diva-25280Local ID: 9720OAI: oai:DiVA.org:liu-25280DiVA: diva2:245608
Available from: 2009-10-07 Created: 2009-10-07 Last updated: 2017-12-13

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Mårdh, Sven

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