Effect of polivalent bothropic antivenom on phospholipase A2, L-Amino acid oxidase and hyaluronidase from peruvian snake venom
DOI:
https://doi.org/10.17843/rpmesp.2008.252.1254Keywords:
Snake venoms, Hyaluronoglucosaminidase, Phospholidases A2, Hialuronidase, L-amino acid oxidase, AntiveninsAbstract
Bothrops sp. snakes causing the largest number of cases of ophidism in Peru, their venom contain several enzymes related to poison spreading, miotoxic and platelet aggregation disturbances. Objectives. The inhibiting capacity of liquid polivalent bothropic antivenom from Instituto Nacional de Salud (INS) has been evaluated on phospholipase A2 (PLA2), L amino acid oxidase (LAO) and hyaluronidase activities using B. atrox, B. barnetti, B. brazili and B. pictus venoms. Material and methods. In each case on 45% egg yolk lipoprotein, Lleucina and O-dianisidine, as well as hyaluronic acid as substrates respectively, using for each enzyme ½, 1 and 2 doses of either natural and heated (37 °C during five days) antivenom, assayed in triplicate. Results. HA was more neutralized enzyme for antivenin, all venoms with the exception of B. brazili were totally inhibited at any dose. For LAO had values of inhibition of 68 to 100% using two doses of the antivenin, PLA2 was the least inhibited (70 to 80%) to two doses. With the heated antivenin was a decline of the inhibitory effect initially found. Conclusions. The measurement of the HA might serve as an indicator of the in vitro potency of antivenins, the bothropic antivenin produced by INS keeping in vitro conditions for inhibition of three major activities of the Peruvian snake venoms.Downloads
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Published
2008-06-30
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Section
Research Articles
How to Cite
1.
Mendoza JC, Lazo F, Yarlequé L, Ruiz NC, Yarlequé A, Pessah S, et al. Effect of polivalent bothropic antivenom on phospholipase A2, L-Amino acid oxidase and hyaluronidase from peruvian snake venom. Rev Peru Med Exp Salud Publica [Internet]. 2008 Jun. 30 [cited 2024 Nov. 21];25(2). Available from: https://rpmesp.ins.gob.pe/index.php/rpmesp/article/view/1254