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Band 3 Protein-Mediated Anion Transport Across the Red Cell Membrane: The Site of Action of the Inhibitors, 4,4′-DI Isothiocyano Dihydrostilbene-2,2′-Disulfonate H2DIDS and 1-Fluoro-2,4-Dinitrobenzene N2ph-F

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

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Kampmann,  Lutz
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Lepke,  Sigrid
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Passow, H., Kampmann, L., & Lepke, S. (1985). Band 3 Protein-Mediated Anion Transport Across the Red Cell Membrane: The Site of Action of the Inhibitors, 4,4′-DI Isothiocyano Dihydrostilbene-2,2′-Disulfonate H2DIDS and 1-Fluoro-2,4-Dinitrobenzene N2ph-F. In A. Pullman (Ed.), Water and Ions in Biological Systems (pp. 385-408). New York: Springer Science+Business Media 1985.


Cite as: https://hdl.handle.net/21.11116/0000-0008-49E9-0
Abstract
Like all other cells, the red blood cells are surrounded by a hydrophobic lipid bilayer that is virtually impermeable for hydro-philic anions such as HCO3− and Cl−. Nevertheless, the HCO3− -Cl− exchange that constitutes an important step in CO2 transport by the blood, is completed within the short time that the red cells pass through the capillary bed of the peripheral tissues or the lung (less than one second). Hence there must exist a transport system that facilitates the anion exchange across the bilayer. This transport system consists of one of the most abundant integral membrane proteins of the red blood cell membrane, the so-called band 3 protein (Cabantchik and Rothstein, 1974; Passow, Fasold, Zaki, Schuhmann and Lepke, 1975).