Purification and properties of a cytolytic toxin in venom of the jellyfish Carybdea marsupialis.

A haemolytic toxin was purified by ion-exchange chromatography and FPLC gel filtration from the nematocysts of the jellyfish Carybdea marsupialis. Sheep red cells, but not human or rabbit red cells, were susceptible to lysis by the toxin. The toxin is a protein with an apparent molecular mass of about 102-107 kDa, is heat labile, highly unstable in polar media, inactivated by reducing agents, and devoid of phospholipase activity. The experimental data speak in favour of a pore-forming mechanism of toxin action.