Abstract
Two toxins, CM-2a and CM-3, were purified from the venom of N. haje annulifera by gel filtration on Sephadex G-50 and by ion-exchange chromatography on CM-cellulose. Whereas toxin CM-2a contains 61 amino acid residues, toxin CM-3 comprises 60 residues. Both toxins are cross-linked by 4 intra-chain disulfide bridges. The complete amino acid sequences of the toxins were elucidated. The properties of the toxins were compared with those of a cytotoxin, a short neurotoxin, a long neurotoxin and an angusticeps type. The sequences of toxin CM-2a and CM-3 and some of the invariant residues do not show a high degree of similarity with those of the other toxins. The toxicities of toxins CM-2a and CM-3 are much lower than those encountered for the cytotoxin or the neurotoxins and their immunochemical properties are distinct from both the cytotoxin and the neurotoxins. They probably represent a new class of toxins.

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