[Properties of phospholipase A2 from the venom of the large hornet Vespa orientalis].
Some properties (catalytic and hemolytic activity, pH and temperature optima, stability, substrate specificity, effects of detergents and metal ions, N-terminal sequence, chemical modification of histidine in the enzyme active center, etc.) of phospholipase A2 from hornet (Vespa orientalis) venom were studied. It was shown that phospholipase A2 from hornet venom differs essentially from other enzymes of this species in terms of stability, catalytic properties and structural features. The active center of the enzyme contains an essential histidine residue, similar to other phospholipases A2 from various sources. Unlike other known forms of phospholipase A2, the enzyme under study exerts a pronounced hemolytic action. The hemolysis is inhibited by Ca2+ at concentrations capable of inducing the activation of the hydrolytic activity of the enzyme.
D000595:Amino Acid Sequence; D000818:Animals; D001514:Bee Venoms / Q000032:analysis*; D001665:Binding Sites; D002118:Calcium / Q000494:pharmacology; D004789:Enzyme Activation; D006461:Hemolysis; D006639:Histidine; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D007928:Lethal Dose 50; D051379:Mice; D010740:Phospholipases / Q000032:analysis*; D010741:Phospholipases A / Q000032:analysis* / Q000378:metabolism / Q000633:toxicity; D054467:Phospholipases A2; D013379:Substrate Specificity; D013696:Temperature; D014862:Wasp Venoms / Q000032:analysis* / Q000378:metabolism / Q000633:toxicity
D001514:Bee Venoms; D014862:Wasp Venoms; D006639:Histidine; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2; D002118:Calcium
Svoĭstva fosfolipazy A2 iz iada bol'shogo shershnia Vespa orientalis.