title: Snake Venoms. Purification, some properties of two phospholipases A2 (CM-I and CM-II) and the amino-acid sequence of CM-II and Bitis nasicornis (horned adder) venom.
abstract: Two phospholipases A2, CM-I and CM-II, were purified from Bitis nasicornis venom by gel filtration on Sephadex G-50, followed by ion-exchange chromatography on CM-cellulose. Both enzymes comprise 119 amino acids, including 12 half-cystine residues. The primary structure of CM-II has been elucidated. The sequence and invariant amino-acid residues of CM-II resemble those of phospholipases A2 from other venoms of Viperidae and Crotalidae (Group II) snake venoms. CM-I and CM-II both contain a single histidine residue which is probably located at the active centre (histidine-47). CM-II are relatively non-toxic.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D010740:Phospholipases / Q000302:isolation & purification*; D010741:Phospholipases A / Q000302:isolation & purification* / Q000378:metabolism; D012910:Snake Venoms / Q000302:isolation & purification; D013045:Species Specificity; D014757:Viper Venoms / Q000302:isolation & purification*
chemical_list: D007527:Isoenzymes; D012910:Snake Venoms; D014757:Viper Venoms; D010740:Phospholipases; D010741:Phospholipases A