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Band‐3 protein‐mediated anion conductance of the red cell membrane

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Kaplan,  Jack H.
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Pring,  M.
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Passow,  Hermann
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Kaplan, J. H., Pring, M., & Passow, H. (1983). Band‐3 protein‐mediated anion conductance of the red cell membrane. FEBS Letters, 156(1), 175-179. doi:10.1016/0014-5793(83)80272-5.


Cite as: http://hdl.handle.net/21.11116/0000-0007-D4AD-7
Abstract
he band 3 protein‐mediated, valinomycin‐induced KCl efflux continues to increase with increasing [KCl] when the Cl/Cl equilibrium exchange becomes saturated. This suggests the existence of a band 3‐mediated component of Cl flux that contributes to the electrical conductance without being related to slippage; i.e., equilibration of the unloaded transport protein between the two membrane surfaces.