Flufenamic acid senses conformation and asymmetry of human erythrocyte band 3 anion transport protein.

@article{Knauf1989FlufenamicAS,
  title={Flufenamic acid senses conformation and asymmetry of human erythrocyte band 3 anion transport protein.},
  author={Philip A. Knauf and Laurie J. Spinelli and Niti Mann},
  journal={The American journal of physiology},
  year={1989},
  volume={257 2 Pt 1},
  pages={C277-89}
}
With Cl as substrate, the human red blood cell anion transport (band 3) protein can exist in four conformations: Ei, with the transport site facing the cytoplasm; Eo, with the transport site facing the external medium; and ECli and EClo, the corresponding forms loaded with Cl. Flufenamic acid (FA), an inhibitor that binds to an external site different from the transport site, binds to Eo with a dissociation constant of 0.0826 +/- 0.0049 (SE) microM. Binding of iodide or sulfate to the external… CONTINUE READING