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Journal Article

The binding of Ca2+ to solubilized band 3 protein of the human erythrocyte membrane

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Passing,  Reinhard
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Schubert,  Dieter
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Passing, R., & Schubert, D. (1983). The binding of Ca2+ to solubilized band 3 protein of the human erythrocyte membrane. Hoppe-Seyler's Zeitschrift für physiologische Chemie, 354(7), 873-878. doi:10.1515/bchm2.1983.364.2.873.


Cite as: https://hdl.handle.net/21.11116/0000-0008-B255-F
Abstract
The binding of 45Ca2+ to isolated band 3 protein, the anion transport protein of the human erythrocyte membrane, was studied by equilibrium dialysis. The protein was solubilized and purified by either the nonionic detergent Ammonyx-L0 or acetic acid. Each preparation of band 3 protein showed a single high-affinity Ca2+ binding site and several Ca2+ binding sites of lower affinity. The association constant of the high-affinity site was 4-13 X 104M-1; it was only moderately dependent on ionic strength. Mg2+ effectively competed with Ca2+ for the site. Anion exchange across the human erythrocyte membrane is inhibited by micromolar concentrations of intracellular Ca2+. Our results suggest that this inhibition is due to the binding of the cation to a single site on band 3 protein.