title: Band 3-hemoglobin associations. The band 3 tetramer is the oxyhemoglobin binding site.
abstract: The associations between the band 3 protein of the human erythrocyte membrane and oxyhemoglobin, in solutions of a nonionic detergent, were studied by sedimentation equilibrium experiments in the analytical ultracentrifuge. The following results were obtained: (i) hemoglobin is bound virtually exclusively to the band 3 tetramer, but not to the monomer or dimer; (ii) the band 3 tetramer can bind up to four hemoglobin tetramers; (iii) unlike the unstable dimers of unmodified band 3, stable dimers crosslinked via S-S-bridges also represent hemoglobin binding sites.
authors.affiliation: Institut für Biophysik der JWG-Universität, Frankfurt am Main, Germany.
authors.forename: P
authors.initials: P
authors.lastname: Schuck
authors.forename: D
authors.initials: D
authors.lastname: Schubert
mesh_terms: D001457:Anion Exchange Protein 1, Erythrocyte / Q000737:chemistry* / Q000302:isolation & purification; D001665:Binding Sites; D003902:Detergents; D004910:Erythrocyte Membrane / Q000737:chemistry; D006454:Hemoglobins / Q000737:chemistry*; D010108:Oxyhemoglobins / Q000737:chemistry; D000077423:Polidocanol; D011092:Polyethylene Glycols; D011487:Protein Conformation; D012996:Solutions
chemical_list: D001457:Anion Exchange Protein 1, Erythrocyte; D003902:Detergents; D006454:Hemoglobins; D010108:Oxyhemoglobins; D012996:Solutions; D000077423:Polidocanol; D011092:Polyethylene Glycols; C100003:deoxyhemoglobin