The chemical, physical and biological properties of the cytolysin tenebrosin-C from Actinia tenebrosa have been compared with those of equinatoxin II from Actinia equina. The two proteins are indistinguishable by reverse-phase and cation-exchange HPLC and capillary zone electrophoresis, and give similar peptide fragments upon cyanogen bromide cleavage (as judged by the chromatographic behaviour, ultraviolet absorption spectra, amino acid composition and N-terminal amino acid sequences of the peptides). Their cardiac stimulatory activities are identical, and their haemolytic activities are similar, with equinatoxin II having slightly greater activity. These data indicate that the two molecules are either identical in all 179 amino acid positions, or differ by no more than one or two residues. These findings are discussed in the context of the taxonomic relationship between the two species of sea anemone.