Comparative Study
doi: 10.1515/bchm2.1981.362.2.997.
Snake venoms. Purification, some properties and amino acid sequence of a phospholipase A2 (DE-I) from Trimeresurus okinavensis (Hime-habu) venom
- PMID: 7275018
- DOI: 10.1515/bchm2.1981.362.2.997
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Comparative Study
Snake venoms. Purification, some properties and amino acid sequence of a phospholipase A2 (DE-I) from Trimeresurus okinavensis (Hime-habu) venom
Hoppe Seylers Z Physiol Chem.
1981 Jul.
Abstract
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.
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