Abstract
Three toxins (CM-2e, CM-4a and CM-7) were purified from the venom of N. haje annulifera by gel filtration on Sephadex and by ion-exchange chromatography on CM-cellulose. They comprise 60 amino acid residues and are cross-linked by 4 intrachain disulfide bridges. The complete amino acid sequences of the 3 toxins were elucidated. The toxicities, the serological properties, the sequences and the invariant amino acid residues of toxin CM-2e, CM-4a and CM-7 resemble the corresponding properties of the cytotoxin group.