High-affinity binding sites for [3H]saxitoxin are associated with voltage-dependent sodium channels in portal vein smooth muscle.

@article{Mironneau1990HighaffinityBS,
  title={High-affinity binding sites for [3H]saxitoxin are associated with voltage-dependent sodium channels in portal vein smooth muscle.},
  author={Jean Mironneau and Catherine Rucker Martin and Serge Arnaudeau and K Jmari and Lala Rakotoarisoa and I Sayet and Chantal Mironneau},
  journal={European journal of pharmacology},
  year={1990},
  volume={184 2-3},
  pages={315-9}
}
Saturable, high-affinity binding sites for [3H]saxitoxin were identified in equine portal vein smooth muscle membranes. These sites had a dissociation constant of 0.29 nM and a maximal binding capacity of 115 fmol.mg-1 of protein. A similar dissociation constant was obtained with cells prepared from rat portal vein. Specific binding of [3H]saxitoxin was completely displaced by unlabelled saxitoxin and tetrodotoxin, with inhibition constants of 0.42 and 2.10 nM, respectively. Tetrodotoxin… CONTINUE READING