Corpus ID: 24677061

Transport-related conformational states of the band 3 protein: probing with 1-fluoro-2,4-dinitrobenzene.

  title={Transport-related conformational states of the band 3 protein: probing with 1-fluoro-2,4-dinitrobenzene.},
  author={W. Ruffing and E. G{\"a}rtner and S. Lepke and B. Legrum and H. Passow},
  journal={Cellular and molecular biology},
  volume={42 7},
The present article provides experimental evidence for previous claims, that Lys 539, without being directly involved in anion binding or translocation, is allosterically linked to the anion binding sites of the band 3 protein and to some other, as yet unidentified amino acid residue. The evidence is based on a detailed study of the kinetics of inhibition of sulphate equilibrium exchange by 1-fluoro-2,4-dinitrobenzene (N2ph-F). It is shown that the mutation of Lys 558 in mouse band 3, which is… Expand
Band 3 Mediated Transport
The band 3 protein is the first member, AE1, of the AE family of anion exchange proteins. The full-length 911 amino acid (Tanner et al. 1988; Lux et al. 1989) version of human AE1 (hAE1) is foundExpand
The structure and function of band 3 (AE1): recent developments (review).
  • M. Tanner
  • Biology, Medicine
  • Molecular membrane biology
  • 1997
Recent advances in understanding of the structure, function and molecular genetics of the membrane domain of red cell anion exchanger, band 3 (AE1), and its role in red cell and kidney disease are discussed. Expand
Hydrodynamic properties of human erythrocyte band 3 solubilized in reduced Triton X-100.
The ability of the different forms of the protein to bind stilbene disulfonates revealed that the dimer had the highest inhibitor binding affinity, and the form characterized by a mean Stokes radius of 114 A to have the lowest. Expand