Revista peruana de medicina experimental y salud publica · 2012
[Variation of the enzymatic activity of Bothrops atrox "jergon" snake venom from three geographic regions, Peru].
Сравнительное исследованиеАннотация на английскомСтатьяПоддержка исследования: вне правительства СШАНазвание и аннотация: Перевод в очереди
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Ortiz César, Lazo Fanny, Bellido Candy, Gonzales Edgar, Yarlequé Armando
Аннотация
OBJECTIVES: To study the variability in the composition and enzymatic activity of venom from adult Bothrops atrox specimens.
MATERIALS AND METHODS: We used venoms from adult snakes from Amazonas, Junín and Ucayali. Each of the venom samples underwent analysis for protein and number of bands by pagesds. Phospholipase A₂, hemolytic, amidolytic, coagulant, hemorrhagic activity were analyzed, also and proteolytic activity on casein and by zymogram. Additionally, immunodiffusion and neutralization assays in vitro were done with a polyvalent botropic serum from the national institute of health of Peru.
RESULTS: The amidolytic, coagulant, hemorrhagic, proteolytic by zymogram, phospholipase A₂, and indirect hemolytic activity were variable, demonstrating increased activity in the venoms from Amazonas, regarding proteolytic by zymogram, phospholipase A₂, and indirect hemolytic activity. While the amount of protein electrophoretic bands and proteolytic activity on casein did not demonstrated differences. Regarding neutralization tests, a 0.5 dose of antivenom was sufficient to effectively neutralize (>50%) the coagulant activity and phospholipase A₂ of all samples analyzed.
CONCLUSIONS: Some biological properties of the venom from adult Bothrops atrox of Peru are variable, without interference with the in vitro neutralization by the polyvalent botropic serum on coagulant and phospholipase A₂ properties of the venom.
MATERIALS AND METHODS: We used venoms from adult snakes from Amazonas, Junín and Ucayali. Each of the venom samples underwent analysis for protein and number of bands by pagesds. Phospholipase A₂, hemolytic, amidolytic, coagulant, hemorrhagic activity were analyzed, also and proteolytic activity on casein and by zymogram. Additionally, immunodiffusion and neutralization assays in vitro were done with a polyvalent botropic serum from the national institute of health of Peru.
RESULTS: The amidolytic, coagulant, hemorrhagic, proteolytic by zymogram, phospholipase A₂, and indirect hemolytic activity were variable, demonstrating increased activity in the venoms from Amazonas, regarding proteolytic by zymogram, phospholipase A₂, and indirect hemolytic activity. While the amount of protein electrophoretic bands and proteolytic activity on casein did not demonstrated differences. Regarding neutralization tests, a 0.5 dose of antivenom was sufficient to effectively neutralize (>50%) the coagulant activity and phospholipase A₂ of all samples analyzed.
CONCLUSIONS: Some biological properties of the venom from adult Bothrops atrox of Peru are variable, without interference with the in vitro neutralization by the polyvalent botropic serum on coagulant and phospholipase A₂ properties of the venom.