Band 3-hemoglobin associations The band 3 tetramer is the oxyhemoglobin binding site

  • Schuck P
  • Schubert D
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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. © 1991.

Author-supplied keywords

  • Analytical ultracentrifugation
  • Band 3 protein
  • Erythrocyte membrane
  • Hemoglobin
  • Protein-protein association

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