A bar model for the pump and channel function of the reconstituted Na+,K+-ATPase |
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Authors: | B M Anner |
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Institution: | Department of Pharmacology, Centre Médical Universitaire, CH-1211 Geneva 4, Switzerland |
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Abstract: | Purified Na+,K+-ATPase is treated with trypsin. The altered enzyme is then reconstituted into liposomes and the change in active and passive Na+,K+-fluxes is recorded. Trypsin treatment transforms the slow passive Na+,K+-fluxes into leaks. The leak formation is correlated with the degree of proteolysis and the associated decrease in Na+,K+-ATPase activity. The active Na+,K+-transport capacity decreases in parallel with the passive transport. It is thus proposed that the Na+,K+-ATPase molecule primarily contains unspecific transmembrane tunnels that are rendered ion-selective by transverse bars of specific length (bar model). |
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Keywords: | Trypsin treatment Reconstitution Membrane leak Bar Model |
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