Interaction between botulinum neurotoxin type A and ganglioside: ganglioside inactivates the neurotoxin and quenches its tryptophan fluorescence.

@article{Kamata1997InteractionBB,
  title={Interaction between botulinum neurotoxin type A and ganglioside: ganglioside inactivates the neurotoxin and quenches its tryptophan fluorescence.},
  author={Yoichi Kamata and Makoto Yoshimoto and Shunji Kozaki},
  journal={Toxicon : official journal of the International Society on Toxinology},
  year={1997},
  volume={35 8},
  pages={1337-40}
}
This study found that ganglioside quenched the tryptophan fluorescence of botulinum neurotoxin type A (BoNT A), accompanied by the inactivation of the toxin under low ionic strength conditions. This finding suggests that the ganglioside-binding site of BoNT A contains tryptophan residues. The quantum yield (a conformation parameter) in BoNT A under high ionic strength conditions differed from that under low ionic strength. This observation indicates that high ionic strength may alter the… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-8 of 8 extracted citations

Handbook of Neurotoxicology

Humana Press • 2002
View 8 Excerpts
Highly Influenced

Molecular Aspects of Botulinum Neurotoxin

Current Topics in Neurotoxicity • 2014
View 3 Excerpts

Similar Papers

Loading similar papers…