| | 1 | Author
| Sabine Lindenthalab, Uwe Scheuringa, H. Orst, R. Ufd, Zbigniew Kojroa, Winfried Haasea, Peter Petraschc, Dieter Schuberta, M. Ikrobiologie0, JohannW. Olfgang, G. | Requires cookie* | | | Title
| Asymmetrie Reconstitution of the Erythrocyte Anion Transport System in Vesicles of Different Curvature: Implications for the Shape of the Band 3 Protein  | | | | Abstract
| The anion transport protein o f the human erythrocyte membrane, band 3, was solubilized and purified in solutions o f 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, 1 2 3 -1 3 5 (1986)). The result ing paucilamellar proteoliposom es o f 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 liposom es obtained had diameters around 32 nm; still smaller vesi cles were free o f protein. All proteoliposom e samples studied showed a rapid sulfate efflux which was sensitive to specific inhibitors o f band 3-mediated anion exchange. In addition, the orientation o f the transport protein in the vesicle membranes was found to be "right-side-out" in all samples. This suggests that the orientation o f the protein in the vesicle membranes is dictated by the shape o f the protein's intramembrane domain and that this domain has the form o f a truncated cone or pyramid. | | | |
Reference
| Z. Naturforsch. 45c, 1021 (1990); received July 18/August 24 1990 | | | |
Published
| 1990 | | | |
Keywords
| Band 3 Protein, A nion Transport System, Asymmetrie Reconstitution, Protein Shape, Erythrocyte Membrane | | | |
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