Characterization of the reversible conformational equilibrium of the cytoplasmic domain of erythrocyte membrane band 3.

@article{Low1984CharacterizationOT,
  title={Characterization of the reversible conformational equilibrium of the cytoplasmic domain of erythrocyte membrane band 3.},
  author={Philip S Low and M A Westfall and David G. Allen and Kenneth C. Appell},
  journal={The Journal of biological chemistry},
  year={1984},
  volume={259 21},
  pages={
          13070-6
        }
}
The cytoplasmic domain of the erythrocyte membrane protein, band 3, contains binding sites for hemoglobin, several glycolytic enzymes, and ankyrin, the linkage to the cytoskeleton. In an earlier study, we found evidence which suggested that band 3 might undergo a native conformational change. We demonstrate here that the cytoplasmic domain of band 3 does exist in a reversible, pH-dependent conformational equilibrium among 3 native states. At physiological salt concentrations this equilibrium is… CONTINUE READING
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