Snake venoms purification some properties of 2 phospho lipases a 2 cm i and cm ii and the amino acid sequence of cm ii from bitis nasicornis horned adder venom
Joubert, F.J.; Townshend, G.S.; Botes, D.P.
Hoppe-Seyler's Zeitschrift fuer Physiologische Chemie 364(12): 1717-1726
Two phospholipases A2, CM-1 and CM-2, were purified from B. nasicornis venom by gel filtration on Sephadex G-50, followed by ion-exchange chromatography on CM-cellulose. Both enzymes comprised 119 amino acids, including 12 half-cystine residues. The primary structure of CM-2 was elucidated. The sequence and invariant amino acid residues of CM-2 resembled those of phospholipases A2 from other venoms of Viperidae and Crotalidae (group 2) snake venoms. CM-1 and CM-2 contained a single His residue which was probably located at the active center (His-47). CM-1 and CM-2 were relatively nontoxic.