The Erythrocyte Anion-Exchange Protein

Primary Structure Deduced from the cDNA Sequence and a Model for Its Arrangement within the Plasma Membrane
  • Ron R. Kopito
  • Harvey F. Lodish
Part of the New Horizons in Therapeutics book series (NHTH)


A full-length cDNA encoding the mouse erythrocyte anion-exchange protein band 3 has been isolated and sequenced. Homology between the amino acid sequence deduced from this cDNA and that of published fragments of human band 3 confirms its identity. A model of the topology of band 3 within the plasma membrane is proposed that is based on published biochemical data and the deduced amino acid sequence. Twelve hydrophobic and amphipathic regions in the anion-exchange domain are proposed to span the membrane as α-helices, resulting in both C and N termini in the interior of the cell. The possibility is considered that these transmembrane helices are organized to form two hydrophilic channels per band 3 monomer, which undergo conformational changes during the anion-exchange cycle.


Anion Transport Cyanogen Bromide Amphipathic Helix Human Erythrocyte Membrane Mouse Erythrocyte 
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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Ron R. Kopito
    • 1
  • Harvey F. Lodish
    • 2
    • 1
  1. 1.Whitehead Institute for Biomedical ResearchCambridgeUSA
  2. 2.Department of BiologyMassachusetts Institute of TechnologyCambridgeUSA

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