Purification of six neurotoxins from the venom of Dendroaspis viridis. Primary structure of two long toxins.

Six neurotoxins were purified from Dendroaspis viridis venom using gel filtration and equilibrium chromatography. The amino acid sequences of two of these neurotoxins (72 and 73 residues, five disulphide bridges) have been determined using almost exclusively automated Edman degradation. These two sequences are very similar: the only differences lies in the presence of one extra glycine at the C-terminal end of one of them. There is a good homology with the sequences of toxins now isolated from other Elapidae and Hydrophidae venoms.