Snake venoms. Purification, some properties and amino acid sequence of a phospholipase A2 (DE-I) from Trimeresurus okinavensis (Hime-habu) venom
Joubert, F.J.; Haylett, T.
Hoppe-Seyler's Zeitschrift für Physiologische Chemie 362(7): 997-1006
ISSN/ISBN: 0018-4888 PMID: 7275018 DOI: 10.1515/bchm2.1981.362.2.997
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.