title: Ultracentrifugation studies on the transmembrane domain of the human erythrocyte anion transporter band 3 in the detergent C12E8.
abstract: The dilute solution behaviour of the transmembrane domain (TMD) of the human erythrocyte anion exchanger Band 3 was studied by analytical ultracentrifugation. Sedimentation velocity and equilibrium studies of the TMD solubilized with the detergent C12E8 demonstrate that the protein is a stable dimer in the concentration range 0.1 to 1 mg/ml. There is no evidence of a dissociation at low concentrations or of an association at higher concentrations. Hydrodynamic calculations applying a prolate ellipsoid of revolution and assuming a hydration of w = 0.35 result in an asymmetrical particle with an axial ratio (a/b) of approximately 3.5.
authors.forename: H
authors.initials: H
authors.lastname: Cölfen
authors.forename: J M
authors.initials: JM
authors.lastname: Boulter
authors.forename: S E
authors.initials: SE
authors.lastname: Harding
authors.forename: A
authors.initials: A
authors.lastname: Watts
mesh_terms: D000465:Algorithms; D001457:Anion Exchange Protein 1, Erythrocyte / Q000737:chemistry*; D003902:Detergents; D006801:Humans; D012996:Solutions; D014461:Ultracentrifugation; D014783:Viscosity
chemical_list: D001457:Anion Exchange Protein 1, Erythrocyte; D003902:Detergents; D012996:Solutions