Joubert F J, Haylett T, Strydom D J, Taljaard N
Hoppe Seylers Z Physiol Chem. 1982 Sep;363(9):1087-96. doi: 10.1515/bchm2.1982.363.2.1087.
Protein CM-2 from Bitis arietans venom was purified by chromatographic procedures involving Sephadex G-50 and CM-cellulose. The purified protein comprises 82 amino acids including 14 half-cystine residues and its primary structure has been elucidated. Protein CM-2 is not toxic. Although the protein clears a suspension of egg yolk, structural features and the inability to hydrolyse L-alpha-lecithin reveal that it cannot be a phospholipase A2. In spite of its sequence showing some homology with that of porcine colipase, protein CM-2 is not a colipase.