Purification and properties of lysophospholipase from the venom of the giant hornet Vespa orientalis

Using biospecific chromatography on polylysocephamide, a toxic phospholipase possessing a presynaptic effect on neuromuscular preparations was isolated from the venom of the giant hornet Vespa orientalis. The enzyme was shown to possess a high hydrolytic activity towards 1-acyllysophosphatidylcholin...

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Bibliographic Details
Published inBiokhimiia (Moscow, Russia) Vol. 53; no. 7; p. 1093
Main Authors Iakubov, I T, Tuĭchibaev, M U, Rakhimov, M M
Format Journal Article
LanguageRussian
Published Russia (Federation) 01.07.1988
Subjects
Bee Venoms - analysis
Catalysis
Detergents
Enzyme Stability
Hemolysis - drug effects
Humans
Hydrogen-Ion Concentration
Hydrolysis
In Vitro Techniques
Kinetics
Lysophospholipase - antagonists & inhibitors
Lysophospholipase - isolation & purification
Lysophospholipase - pharmacology
Phospholipases - isolation & purification
Temperature
Wasp Venoms - analysis
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Summary:Using biospecific chromatography on polylysocephamide, a toxic phospholipase possessing a presynaptic effect on neuromuscular preparations was isolated from the venom of the giant hornet Vespa orientalis. The enzyme was shown to possess a high hydrolytic activity towards 1-acyllysophosphatidylcholine within a narrow pH range (pH optimum 7.5). The enzyme activity was suppressed by detergents of various chemical composition. Lysophospholipase caused an intensive hemolysis of washed human erythrocytes. The catalytic and hemolytic functions of the enzyme were sensitive to metal ions, however, in a different degree. Ca2+ and Mn2+ activated, while Cu2+ and Zn2+ inhibited the enzyme. Mg2+ and Sr2+ had no effect on the enzyme activity.
ISSN:0320-9725