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Kinetics of pump currents generated by the Na+,K+-ATPase

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Fendler,  Klaus
Transport Proteins Group, Max Planck Institute of Biophysics, Max Planck Society;

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Grell,  Ernst
Molecular Biophysics Group, Max Planck Institute of Biophysics, Max Planck Society;

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Bamberg,  Ernst
Transport Proteins Group, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Fendler, K., Grell, E., & Bamberg, E. (1987). Kinetics of pump currents generated by the Na+,K+-ATPase. FEBS Letters, 224(1), 83-88. doi:10.1016/0014-5793(87)80427-1.


Cite as: http://hdl.handle.net/21.11116/0000-0007-933B-1
Abstract
Purified Na+,K+-ATPase from pig kidney was attached to black lipid membranes. Pump currents of the enzyme could be measured with a time resolution of approx. 1 ms by releasing ATP from caged ATP with a UV laser flash. Analysis of the transient currents shows that a slow non-electrogenic step is followed by an electrogenic transition with a rate constant of 100 s-1 (22 degrees C). The exponential components found in the transient currents are compared to transitions in the Albers-Post scheme.