Characterization of ten proteins from the venom of the Moroccan scorpion Androctonus mauretanicus mauretanicus, six of which are toxic to the mouse.

When the venom of the scorpion Androctonus mauretanicus mauretanicus was submitted to purification procedures, ten proteins were obtained; six were lethal to mice and four were devoid of toxicity in the biological tests used. The ten molecules were characterized by their amino acid composition, and among them toxin V and polypeptide P2 by their amino acid sequences. Peptide P2 (35 amino acid residues), a structural homologue of the so called Buthus epeus short 'insectotoxins' I1 and I5, was inactive on fly larvae and absent from the 'manual venom' obtained by manual handling and excitation of the scorpions.