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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

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.

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 Creators:
Lindenthal, Sabine1, 2, Author              
Scheuring, Uwe1, Author              
Ruf, Horst3, Author              
Kojro, Zbigniew3, Author              
Haase, Winfried4, Author              
Petrasch, Peter5, Author
Schubert, Dieter1, 2, Author              
Affiliations:
1Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_3264817              
2Institut für Biophysik, Johann Wolfgang Goethe-Universität, Frankfurt am Main, Germany, ou_persistent22              
3Molecular Biophysics Group, Max Planck Institute of Biophysics, Max Planck Society, ou_3264820              
4Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068297              
5Institut für Mikrobiologie, Johann Wolfgang Goethe-Universität, Frankfurt am Main, Germany, ou_persistent22              

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Free keywords: Band 3 Protein; Anion Transport System; Asymmetrie Reconstitution; Erythrocyte Membrane
 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.

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Language(s): eng - English
 Dates: 1990-07-181990-08-2420151990-10-01
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1515/znc-1990-9-1014
PMID: 2291767
 Degree: -

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Title: Zeitschrift für Naturforschung, C: Journal of Biosciences
  Abbreviation : Z. Naturforsch., C: J. Biosci.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Berlin : Walter de Gruyter GmbH
Pages: - Volume / Issue: 45c (9-10) Sequence Number: - Start / End Page: 1021 - 1026 Identifier: ISSN: 1865-7125
CoNE: https://pure.mpg.de/cone/journals/resource/954927655916_1