Snake Venoms. Purification, some Properties of Two Phospholipases A2(CM-I and CM-II) and the Amino-Acid Sequence of CM-II fromBitis nasicornis(Horned Adder) Venom
- 1 January 1983
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 364 (2) , 1717-1726
- https://doi.org/10.1515/bchm2.1983.364.2.1717
Abstract
Two phospholipases A2, CM-1 and CM-2, were purified from B. nasicornis venom by gel filtration on Sephadex G-50, followed by ion-exchange chromatography on CM-cellulose. Both enzymes comprised 119 amino acids, including 12 half-cystine residues. The primary structure of CM-2 was elucidated. The sequence and invariant amino acid residues of CM-2 resembled those of phospholipases A2 from other venoms of Viperidae and Crotalidae (group 2) snake venoms. CM-1 and CM-2 contained a single His residue which was probably located at the active center (His-47). CM-1 and CM-2 were relatively nontoxic.This publication has 16 references indexed in Scilit:
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