Anion transport across the red blood cell membrane and the protein in band 3.
The paper reviews existing evidence for the participation of the protein in band 3 (nomenclature of Steck, [1]) in anion transport across the red cell membrane and discusses the possible role of common binding sites on band 3 for 1-fluoro-2,4-dinitrobenzene, 2-(4'-aminophenyl)-6-methylbenzenethiazol-3',7-disulfonic acid and dihydro 4,4'-diisothiocyanato stilbene-2,2'-disulfonic acid in the transport process.
D000345:Affinity Labels; D000838:Anions; D001557:Benzenesulfonates / Q000378:metabolism; D001665:Binding Sites; D001692:Biological Transport; D001798:Blood Proteins / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism; D004139:Dinitrofluorobenzene / Q000378:metabolism; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism*; D008081:Liposomes; D008565:Membrane Proteins / Q000378:metabolism*; D013267:Stilbenes / Q000378:metabolism; D013844:Thiazoles / Q000378:metabolism
D000345:Affinity Labels; D000838:Anions; D001557:Benzenesulfonates; D001798:Blood Proteins; D002352:Carrier Proteins; D006023:Glycoproteins; D008081:Liposomes; D008565:Membrane Proteins; D013267:Stilbenes; D013844:Thiazoles; D004139:Dinitrofluorobenzene