Characterization of the pH dependence of hemoglobin binding to band 3. Evidence for a pH-dependent conformational change within the hemoglobin-band 3 complex.

@article{Salhany1998CharacterizationOT,
  title={Characterization of the pH dependence of hemoglobin binding to band 3. Evidence for a pH-dependent conformational change within the hemoglobin-band 3 complex.},
  author={J. Mitchell Salhany and Karen A. Cordes and Renee L. Sloan},
  journal={Biochimica et biophysica acta},
  year={1998},
  volume={1371 1},
  pages={
          107-13
        }
}
The pH dependence of hemoglobin binding to inside-out red cell membrane vesicles was studied using 90 degrees light scattering (Salhany, J.M. et al., Biochemistry 19 (1980) 1447-1454). Hyperbolic binding curves were observed for high-affinity hemoglobin binding to the cytoplasmic domain of band 3 (CDB3) within the intact transporter. Analysis of these saturation curves yielded the apparent Kd and the maximum light scattering signal change (DeltaLSmax ). The apparent Kd for hemoglobin binding… CONTINUE READING

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