The kaliotoxin family enlarged. Purification, characterization, and precursor nucleotide sequence of KTX2 from Androctonus australis venom.

@article{Fatima1994TheKF,
  title={The kaliotoxin family enlarged. Purification, characterization, and precursor nucleotide sequence of KTX2 from Androctonus australis venom.},
  author={Laraba-Djebari Fatima and Christian Legros and Marcel Crest and Brigitte C{\'e}ard and R Romi and P Mansuelle and Guy Jacquet and Jurphaas van Rietschoten and Maurice Gola and Herv{\'e} Rochat},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 52},
  pages={32835-43}
}
Kaliotoxin (KTX) has been originally described as an inhibitor of the intermediate conductance Ca(2+)-activated K+ channel (Crest, M., Jacquet, G., Gola, M., Zerrouk, H., Benslimane, A., Rochat, H., Mansuelle, P., and Martin-Eauclaire, M.-F. (1992) J. Biol. Chem. 267, 1640-1647). However, the radioiodinated 125I-KTX-(1-37) was also able to bind to the dendrotoxin sensitive voltage-dependent K+ channel (Romi, R., Crest, M., Gola, M., Sampieri, F., Jacquet, G., Zerrouk, H., Mansuelle, P… CONTINUE READING
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