title: Snake venom: protein CM-2 from Bitis arietans (puff adder) venom.
abstract: 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.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D036341:Intercellular Signaling Peptides and Proteins; D007700:Kinetics; D008049:Lipase / Q000302:isolation & purification / Q000378:metabolism; D010446:Peptide Fragments / Q000032:analysis; D010741:Phospholipases A / Q000302:isolation & purification / Q000378:metabolism; D054467:Phospholipases A2; D011506:Proteins / Q000302:isolation & purification*; D012911:Snakes; D014357:Trypsin; D014757:Viper Venoms / Q000302:isolation & purification*
chemical_list: C036113:CM-2 protein, Bitis arietans; D036341:Intercellular Signaling Peptides and Proteins; D010446:Peptide Fragments; D011506:Proteins; D014757:Viper Venoms; D008049:Lipase; D010741:Phospholipases A; D054467:Phospholipases A2; D014357:Trypsin