Snake venoms. Purification, some properties and amino acid sequence of a phospholipase A2 (DE-I) from Trimeresurus okinavensis (Hime-habu) venom.
A phospholipase A2 (DE-I) was purified from Trimeresurus okinavensis (Hime-habu) venom by gel filtration on Sephadex G-50 followed by ion-exchange chromatography on DEAE-cellulose. It comprises 123 amino acid residues including 14 half-cystine residues. The primary structure of the enzyme has been elucidated. The sequence and invariant amino acid residues of DE-I resemble those of phospholipases A2 from venoms of Viperidae and Crotalidae (Group II) snake venoms. The phospholipase A2 from T. okinavensis contains two histidine residues which are located at the N-terminal residue and at the active centre (histidine-47). The acidic phospholipase A2 (DE-I) is not toxic.
D000595:Amino Acid Sequence; D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002918:Chymotrypsin; D003435:Crotalid Venoms / Q000302:isolation & purification*; D010446:Peptide Fragments / Q000032:analysis; D010740:Phospholipases / Q000302:isolation & purification*; D010741:Phospholipases A / Q000302:isolation & purification*; D054467:Phospholipases A2; D013045:Species Specificity; D014357:Trypsin
D003435:Crotalid Venoms; D010446:Peptide Fragments; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2; D002918:Chymotrypsin; D014357:Trypsin