title: Reconstitution of the erythrocyte anion channel.
abstract: Band 3, the membrane protein which mediates erythrocyte anion exchange, was purified on a concanavalin A column. Triglycerides, diglycerides, cholesteryl esters, cholesterol, and phosphatidylcholine were found to copurify. The column product gave at least two and probably three bands by isoelectric focusing. Antibodies prepared against the purified Band 3 appeared to react only with the cytoplasmic face of Band 3. Vesicles prepared with Band 3 had an accelerated uptake of SO4(2-) which could be inhibited by 2-(j'-aminophenyl)-6-methyl benzene thiazo-3', 7-disulfonic acid, a potent inhibitor of anion transport in the intact system. The possible source of this difference is discussed. Band 3 was spin labeled, probably at one specific site. The spectra showed that the spin label was highly immobilized, but no dipole-dipole interactions between spin labels on adjacent Band 3 subunits were apparent.
mesh_terms: D000838:Anions; D000906:Antibodies; D001557:Benzenesulfonates / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000187:drug effects; D004912:Erythrocytes / Q000378:metabolism; D005033:Ethylmaleimide / Q000494:pharmacology; D006021:Glycophorins / Q000302:isolation & purification; D006801:Humans; D007474:Ion Exchange; D008565:Membrane Proteins / Q000097:blood* / Q000276:immunology / Q000302:isolation & purification; D011952:Receptors, Concanavalin A / Q000302:isolation & purification; D013844:Thiazoles / Q000494:pharmacology
chemical_list: D000838:Anions; D000906:Antibodies; D001557:Benzenesulfonates; D006021:Glycophorins; D008565:Membrane Proteins; D011952:Receptors, Concanavalin A; D013844:Thiazoles; D005033:Ethylmaleimide