Characterization of high affinity binding sites for charybdotoxin in human T lymphocytes. Evidence for association with the voltage-gated K+ channel.

@article{Deutsch1991CharacterizationOH,
  title={Characterization of high affinity binding sites for charybdotoxin in human T lymphocytes. Evidence for association with the voltage-gated K+ channel.},
  author={Carol Deutsch and Max Price and S Lee and V. Frank King and M. L. Garcia},
  journal={The Journal of biological chemistry},
  year={1991},
  volume={266 6},
  pages={3668-74}
}
Charybdotoxin (ChTX) inhibits with high affinity a voltage-gated K+ channel that is present in human T lymphocytes. In this system, 125I-ChTX binds specifically and reversibly to a single class of sites which display a Kd of 8-14 pM, as measured by either equilibrium or kinetic binding protocols. The maximum density of sites, 542 sites/cell, correlates well with the density of K+ channel as determined by electrophysiological experiments. Binding of 125I-ChTX is modulated by the ionic strength… CONTINUE READING