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Asymmetric reconstitution of the erythrocyte anion transport system in vesicles of different curvature: implications for the shape of the band 3 protein

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Lindenthal,  Sabine
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;
Institut für Biophysik, Johann Wolfgang Goethe-Universität, Frankfurt am Main, Germany;

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Scheuring,  Uwe
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Ruf,  Horst
Molecular Biophysics Group, Max Planck Institute of Biophysics, Max Planck Society;

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Kojro,  Zbigniew
Molecular Biophysics Group, Max Planck Institute of Biophysics, Max Planck Society;

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Haase,  Winfried
Department of 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;
Institut für Biophysik, Johann Wolfgang Goethe-Universität, Frankfurt am Main, Germany;

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Citation

Lindenthal, S., Scheuring, U., Ruf, H., Kojro, Z., Haase, W., Petrasch, P., et al. (1990). Asymmetric reconstitution of the erythrocyte anion transport system in vesicles of different curvature: implications for the shape of the band 3 protein. Zeitschrift für Naturforschung, C: Journal of Biosciences, 45c(9-10), 1021-1026. doi:10.1515/znc-1990-9-1014.


Cite as: http://hdl.handle.net/21.11116/0000-0008-185D-6
Abstract
The anion transport protein of the human erythrocyte membrane, band 3, was solubilized and purified in solutions of the non-ionic detergent nonaethylene glycol lauryl ether and then reconstituted in spherical egg phosphatidylcholine bilayers as described earlier (U. Scheuring, K. Kollewe, W. Haase, and D. Schubert, J. Membrane Biol. 90, 123-135 (1986)). The resulting paucilamellar proteoliposomes of average diameter 70 nm were transformed into smaller vesicles by French press treatment and fractionated according to size by gel filtration. The smallest protein-containing liposomes obtained had diameters around 32 nm; still smaller vesicles were free of protein. All proteoliposome samples studied showed a rapid sulfate efflux which was sensitive to specific inhibitors of band 3-mediated anion exchange. In addition, the orientation of the transport protein in the vesicle membranes was found to be "right-side-out" in all samples. This suggests that the orientation of the protein in the vesicle membranes is dictated by the shape of the protein's intramembrane domain and that this domain has the form of a truncated cone or pyramid.