Binding of a radiolabeled sea anemone cytolysin to erythrocyte membranes.

@article{Doyle1989BindingOA,
  title={Binding of a radiolabeled sea anemone cytolysin to erythrocyte membranes.},
  author={J. William Doyle and William R. Kem},
  journal={Biochimica et biophysica acta},
  year={1989},
  volume={987 2},
  pages={181-6}
}
Stichodactyla helianthus cytolysin III, a 17 kDa basic polypeptide isolated from a Caribbean sea anemone, is one of the most potent hemolysins yet found in a living organism. This toxin has been reported to form new ion channels in artificial lipid bilayer membranes. The ability of this toxin to attack cell membranes is greatly enhanced by the presence of sphingomyelin. In order to investigate the mechanism by which the cytolysin causes cell lysis, we have prepared a highly active [3H]cytolysin… CONTINUE READING