A role for band 4.2 in human erythrocyte band 3 mediated anion transport

Affinity chromotography is used to purify human erythrocyte band 3 and band 4.2 peripheral proteins. Liposomes of the lipid group are formed from band 3 protein and exhibit a ratio resembling that of erythrocyte membranes. The working and proper organization of the protein are examined by employing stilbenedisulfonate prevention of band 3 controlled efflux of radiolabeled sulfate from preloaded liposomes. A distinct variation in efflux is observed when sulfate efflux controlled by purified band 3 and incompletely purified band 3 constituting sample quantities of bands 4.1 and 4. 2 are compared.