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- W1993120216 abstract "The relation between the enzymatic activity and the potent toxicity to arthropods of the basic phospholipase P3 (Ph A2-P3) derived from the venom of the South African Cobra Naja mossambica mossambica was investigated. It was found that: 1.(1) There was no correlation between the toxic and the enzymatic activities of several pure phospholipases derived from different biological sources;2.(2) There was no preference by the Ph A2-P3 for substrates originating from tissues of the respective test animals;3.(3) Accumulation of lysophosphatides in the Ph A2-P3 haemolymph incubation mixture did not result in an increase in the toxic potency;4.(4) Pure lysolecithin had a relatively low lethal potency;5.(5) Addition of cardiotoxin, derived from the same venom, did not increase the toxic potency of Ph A2-P3;6.(6) Inactivation experiments of the Ph A2-P3 by heat treatment at different pH conditions resulted in an identical decrease in both toxicity and phospholipase activity;7.(7) The employment of reagent p-bromophenacyl bromide, known as a specific inhibitor of phospholipase A2, resulted in an identical rate of inactivation of the toxic as well as enzymatic activity;8.(8) A series of assays performed in the p-bromophenacyl bromide modified Ph A2-P3, with regard to its biological activities, amino acid composition, chromatographical mobility, u.v. spectrum and amino acid analysis, have indicated a specific blockage of the enzymatic catalytic site.It may be concluded that the toxicity of Ph A2-P3 to arthropods is not mediated by a general release of lysophosphatides or cooperative interactions with other venom components but is directly associated to the enzymatic action of the phospholipase." @default.
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- W1993120216 date "1981-01-01" @default.
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- W1993120216 title "Cobra venom phospholipase highly toxic to arthropods—II relation between toxicity and enzymatic activity" @default.
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- W1993120216 doi "https://doi.org/10.1016/0020-1790(81)90087-1" @default.
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