Snake Venoms. Purification, some Properties and Amino Acid Sequence of a Phospholipase A2(DE-I) fromTrimeresurus okinavensis(Hime-habu) Venom
- 1 January 1981
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 362 (2), 997-1006
- https://doi.org/10.1515/bchm2.1981.362.2.997
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 2 histidine residues which are located at the N-terminal residue and at the active center (histidine-47). The acidic phospholipase A2 (DE-I) is not toxic.This publication has 12 references indexed in Scilit:
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