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Mediation of inorganic anion transport by the hydrophobic domain of mouse erythroid band 3 protein expressed in oocytes of Xenopus laevis

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

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Becker,  Anja
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

Lepke, S., Becker, A., & Passow, H. (1992). Mediation of inorganic anion transport by the hydrophobic domain of mouse erythroid band 3 protein expressed in oocytes of Xenopus laevis. Biochimica et Biophysica Acta-Biomembranes, 1106(1), 13-16. doi:10.1016/0005-2736(92)90215-8.


Cite as: http://hdl.handle.net/21.11116/0000-0007-CD48-2
Abstract
A cDNA clone of the mouse erythroid band 3 protein encoding the 556 amino acid residues of the hydrophobic domain from Thr-374 to the C-terminal Val-929 is shown by immunoprecipitation to be expressed in Xenopus oocytes. Measurements of 36Cl- efflux indicate that the translation product mediates Cl- transport, which is inhibitable reversibly by DNDS or H2DIDS, specific inhibitors of band 3-mediated transport. The apparent KI values are 3.6 microM and 0.094 microM, respectively, and hence similar to those found in the wild type band 3-mediated anion transport. The rapid reversible inhibition by H2DIDS slowly changes to irreversible inhibition. The rate of change increases with increasing pH, again similar as to the wild-type band 3. It is concluded that the hydrophobic domain of band 3 is capable of executing anion transport essentially similar to the full-length band 3, although minor differences with respect to transport and inhibition kinetics cannot be ruled out.