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Título: Neutralization of pharmacological and toxic activities of Bothrops jararacussu snake venom and isolated myotoxins by Serjania erecta methanolic extract and its fractions
Palavras-chave: Snake venom
Medicinal plants
Antiophidian properties
Serjania erecta
Bothrops jararacussu
Myotoxins
Data do documento: 2011
Editor: Universidade Estadual Paulista Júlio de Mesquita Filho (UNESP), Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP) - Câmpus de Botucatu
Citação: FERNANDES, R. S. et al. Neutralization of pharmacological and toxic activities of Bothrops jararacussu snake venom and isolated myotoxins by Serjania erecta methanolic extract and its fractions. Journal of Venomous Animals and Toxins including Tropical Diseases, Botucatu, v. 17, n. 1, p. 85-93, 2011. DOI: 10.1590/S1678-91992011000100011.
Resumo: Most of the snakebites recorded in Brazil are caused by the Bothrops genus. Given that the local tissue damage caused by this genus cannot be treated by antivenom therapy, numerous studies are focusing on supplementary alternatives, such as the use of medicinal plants. Serjania erecta has already demonstrated anti-inflammatory, antiseptic and healing properties. In the current study, the aerial parts of S. erecta were extracted with methanol, then submitted to chromatographic fractionation on a Sephadex LH20 column and eluted with methanol, which resulted in four main fractions. The crude extract and fractions neutralized the toxic activities of Bothrops jararacussu snake venom and isolated myotoxins (BthTX-I and II). Results showed that phospholipase A2, fibrinogenolytic, myotoxic and hemorrhagic activities were inhibited by the extract. Moreover, the myotoxic and edematous activities induced by BthTX-I, and phospholipase A2 activity induced by BthTX-II, were inhibited by the extract of S. erecta and its fraction. The clotting time on bovine plasma was significantly prolonged by the inhibitory action of fractions SF3 and SF4. This extract is a promising source of natural inhibitors, such as flavonoids and tannins, which act by forming complexes with metal ions and proteins, inhibiting the action of serineproteases, metalloproteases and phospholipases A2.
URI: http://repositorio.ufla.br/jspui/handle/1/40996
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