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.
|Translated title of the contribution||Variation of the enzymatic activity of Bothrops atrox "Jergon" snake venom from three geographic regions, Peru|
|Number of pages||8|
|Journal||Revista Peruana de Medicina Experimental y Salud Publica|
|State||Published - 2012|
- Snake venoms