alpha-Haemolysin is a protein toxin (107 kDa) secreted by some pathogenic strains of E. coli. It binds to mammalian cell membranes, disrupting cellular activities and lysing cells. This paper describes the mechanism of alpha-haemolysin-induced membrane leakage, from experiments in which extrusion large unilamellar vesicles, loaded with fluorescent solutes, are treated with purified toxin. The results show that the toxin does not require of any membrane receptor to exert its activity, that vesicles become leaky following an 'all-or-none' mechanism, and that leakage occurs through a non-osmotic detergent-like bilayer disruption induced by the protein. Small pores formed by monomeric alpha-haemolysin, as described by other authors, do not appear to be related to the process of membrane disruption. Instead, the experimental data would be in agreement with the idea of oligomeric assemblies being required to produce release of solutes from a single vesicle.