title: The complete amino-acid sequence of a basic phospholipase A2 in the venom of Bungarus fasciatus.
abstract: A basic phospholipase A2 (PLA2) was isolated and purified from the venom of Bungarus fasciatus. Four kinds of enzymes, lysyl endopeptidase, endoproteinase Asp-N, endoproteinase Glu-C and trypsin, were employed to elucidate the complete primary structure by means of gas-phase sequencing. The amino-acid sequence reveals 118 amino-acid residues containing seven pairs of half-cystine. It has 78% and 61% structural identities with PLA2 from Bungarus multicinctus and Naja melanoleuca DE-II, respectively.
authors.affiliation: Institute of Biological Chemistry, Academia Sinica, National Taiwan University.
authors.forename: C S
authors.initials: CS
authors.lastname: Liu
authors.forename: C S
authors.initials: CS
authors.lastname: Chang
authors.forename: H L
authors.initials: HL
authors.lastname: Leu
authors.forename: S W
authors.initials: SW
authors.lastname: Chen
authors.forename: T B
authors.initials: TB
authors.lastname: Lo
mesh_terms: D000595:Amino Acid Sequence; D002038:Bungarotoxins; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D010447:Peptide Hydrolases; D010740:Phospholipases / Q000302:isolation & purification; D010741:Phospholipases A / Q000302:isolation & purification; D054467:Phospholipases A2
chemical_list: D002038:Bungarotoxins; D010446:Peptide Fragments; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2; D010447:Peptide Hydrolases