ASYMMETRIC AND FUNCTIONAL RECONSTITUTION OF BAND-3 INTO PREFORMED PHOSPHATIDYLCHOLINE VESICLES

Human erythrocyte band 3 protein was purified in 0.1% Triton X-100 and reconstituted into pre-formed phosphatidylcholine vesicles by a Trito n X-100-mediated procedure [1]. Band 3 (and its transmembrane domain) could be asymmetrically reconstituted into phosphatidylcholine vesicle s with retention of sulfate transport activity which showed behaviour characteristic of red cell anion transport in response to pH, H2DIDS a nd temperature. Successful reconstitution was also possible using high mol ratios of band 3/phosphatidylcholine (1:200), which are not achie ved by any other method.