title: Naja mossambica mossambica venom. Purification, some properties and the amino acid sequences of three phospholipases A (CM-I, CM-II and CM-III).
abstract: Three phospholipases A, CM-I, CM-II and CM-III, were purified from Naja mossambica mossambica venom by gel filtration on Sephadex G-50 followed by ion-exchange chromatography on CM-cellulose. They comprise each 118 amino acid residues and are close-linked by seven intrachain disulphide bridges. The complete primary structure of the three phospholipases A have been elucidated. The sequences and the invariant amino acid residues of CM-I, CM-II and CM-III resemble those of phospholipases A from other snake venoms and also from porcine pancreas. However, the letality (LD50 values) of the three phospholipases A from Naja mossambica mossambica venom, differ among themselves, and are also much higher than the LD100 value encountered for notexin from Notechis scutatus scutatus venom.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D010446:Peptide Fragments / Q000032:analysis; D010740:Phospholipases / Q000302:isolation & purification / Q000378:metabolism; D012910:Snake Venoms; D013045:Species Specificity
chemical_list: D000596:Amino Acids; D007527:Isoenzymes; D010446:Peptide Fragments; D012910:Snake Venoms; D010740:Phospholipases