Abstract
Four toxins (CM-7, CM-8, CM-9 and CM-10b) were purified from Naja haje haje (Egyptian cobra) venom by gel filtration on Sephadex G-50 followed by ion-exchange chromatography on CM-cellulose. They each contain 60 amino acid residues and are cross-linked by four intrachain disulphide bridges. The complete primary structure of the four toxins have been elucidated. The toxicities, the immunochemical properties, the sequences and the invariant amino acid residues of toxins CM-7, CM-8, CM-9 and CM-10b resemble the corresponding properties of the cytotoxin group.
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