Volume 103, Issue 1 pp. 104-107

Neutralization of Pharmacological and Toxic Activities of Bothrops Snake Venoms by Schizolobium parahyba (Fabaceae) Aqueous Extract and Its Fractions

Luis Henrique F. Vale

Luis Henrique F. Vale

Institute of Genetic and Biochemical, University of Uberlândia, UFU, Uberlândia/MG, Brazil, and

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Mirian M. Mendes

Mirian M. Mendes

Institute of Genetic and Biochemical, University of Uberlândia, UFU, Uberlândia/MG, Brazil, and

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Amélia Hamaguchi

Amélia Hamaguchi

Institute of Genetic and Biochemical, University of Uberlândia, UFU, Uberlândia/MG, Brazil, and

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Andreimar M. Soares

Andreimar M. Soares

Department of Clinical, Toxicological and Bromatological Analysis, Faculty of Pharmaceutical Sciences of Ribeirão Preto, São Paulo University, FCFRP-USP, Ribeirão Preto, Brazil

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Veridiana M. Rodrigues

Veridiana M. Rodrigues

Institute of Genetic and Biochemical, University of Uberlândia, UFU, Uberlândia/MG, Brazil, and

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Maria Inês Homsi-Brandeburgo

Maria Inês Homsi-Brandeburgo

Institute of Genetic and Biochemical, University of Uberlândia, UFU, Uberlândia/MG, Brazil, and

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First published: 28 June 2008
Citations: 25
Author for correspondence: Veridiana M. Rodrigues, Laboratório de Química de Proteínas e Produtos Naturais, Instituto de Genética e Bioquímica, Universidade Federal de Uberlândia, Campus Umuarama, Bloco 2E sala 32E, 38400-902 Uberlândia-MG, Brazil (fax 0055 3432182203#24, e-mail [email protected]).

Abstract

Abstract: The aqueous extract prepared from Schizolobium parahyba (Sp) leaves, a native plant from Atlantic Forest (Brazil), was tested to analyse its ability to inhibit some biological and enzymatic activities induced by Bothrops alternatus (BaltCV) and Bothrops moojeni (BmooCV) snake venoms. Sp inhibited 100% of lethality, blood incoagulability, haemorrhagic and indirect haemolytic activities at a 1:10 ratio (venom/extract, w/w), as well as coagulant activity at a 1:5 ratio (venom/extract, w/w) induced by both venoms. BaltCV fibrinogenolytic activity was also neutralized by Sp at a 1:10 ratio, resulting in total protection of fibrinogen Bβ chain and partial protection of Aα chain. Interaction tests have demonstrated that, at certain extract/proteins ratios, Sp precipitates proteins non-specifically suggesting the presence of tannins, which are very likely responsible for the excellent inhibiting effects of the analysed ophidian activities. Sp aqueous extract chromatography on Sephadex LH-20 was carried out aiming at the separation of these compounds that mask the obtained results. Thus, the fractionation of Sp resulted in three fractions: F1 (methanolic fraction); F2 (methanol:water fraction, 1:1 v/v); and F3 (aqueous fraction). These fractions were analysed for their ability to inhibit the BaltCV fibrinogenolytic activity. F1 inhibited 100% the venom fibrinogenolytic activity without presenting protein precipitation effect; F2 showed only partial inhibition of this venom activity. Finally, F3 did not inhibit fibrinogen proteolysis, but presented strong protein precipitating action. We conclude that Sp aqueous extract, together with tannins, also contains other compounds that can display specific inhibitory activity against snake venom toxins.

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