Analysis of the blocking activity of charybdotoxin homologs and iodinated derivatives against Ca2+-Activated K+ channels

@article{Lucchesi1989AnalysisOT,
  title={Analysis of the blocking activity of charybdotoxin homologs and iodinated derivatives against Ca2+-Activated K+ channels},
  author={Kathryn Lucchesi and Arippa Ravindran and H. Young and Edward G. Moczydlowski},
  journal={The Journal of Membrane Biology},
  year={1989},
  volume={109},
  pages={269-281}
}
Two charybdotoxin peptides were purified from venom of the Israeli scorpion,Leiurus quinquestriatus hebraeus. Microsequencing of the most abundant toxin, ChTX-Lq1, revealed identity with the 37-residue peptide previously sequenced by Gimenez-Gallego et al. [Gimenez-Gallego, G., et al.,Proc. Natl. Acad. Sci. USA 85:3329–3333 (1988)]. Sequence data on the minor peptide, ChTX-Lq2, showed substantial homology to ChTX-Lq1 with differences observed at eight positions. These two charybdotoxin… CONTINUE READING

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Iodine-Labeled Plasma Proteins

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Highly Influential
4 Excerpts

Block of K(Ca) channels by mono-iodinated charybdotoxin derivatives and a newly identified homolog

  • K. J. Lucchesi, E. Moczydlowski
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  • 1989
1 Excerpt

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