TY  - JOUR
A1  - Lindenthal, Sabine
A1  - Scheuring, Uwe
A1  - Ruf, Horst
A1  - Kojro, Zbigniew
A1  - Haase, Winfried
A1  - Petrasch, Peter
A1  - Schubert, Dieter
T1  - Asymmetric reconstitution of the erythrocyte anion transport system in vesicles of different curvature: implications for the shape of the band 3 protein
T2  - Zeitschrift für Naturforschung, C
N2  - 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 proteoliposom es 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.
KW  - Band 3 Protein
KW  - Anion Transport System
KW  - Asymmetrie Reconstitution
KW  - Protein Shape
KW  - Erythrocyte Membrane
Y1  - 2014
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/79922
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-799224
SN  - 0939-5075
SN  - 1865-7125
VL  - 45.1990
IS  - 9-10
SP  - 1021
EP  - 1026
PB  - Verlag der Zeitschrift für Naturforschung
CY  - Tübingen
ER  -