Snake Venom Toxins

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Abstract
Twelve low-molecular-weight proteins, of which eleven have subcutaneous LD50 values of less than 40 μg/g mouse, were purified from Dendroaspis polylepis polvlepis venom. Ion-exchange chromatography on Amberlite CG-50 and ion-exchange chromatography on carboxymethylcellulose and/or phosphocellulose was used for the purification. The amino-terminal sequences of these proteins were determined and used to indicate that five groups of low-molecular-weight polypeptides are to be found in black mamba venom. Proteins from two of these groups which have low toxicity individually, when used together show synergism, in that their toxicity in combination is greater than the sum of their individual toxicities.