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Antiophidian properties of plant extracts against Lachesis muta venom J. Venom. Anim. Toxins incl. Trop. Dis.
De Paula,RC; Sanchez,EF; Costa,TR; Martins,CHG; Pereira,PS; Lourenço,MV; Soares,AM; Fuly,AL.
Snakebites comprise a serious health problem in several countries due to their global incidence, which exceeds 2.5 million per year, and the elevated number of victim fatalities. To counteract envenomations, antivenoms have been used regularly for more than a century. Apart from side effects including anaphylactic reactions, antivenoms are not able to efficiently neutralize local tissue damage, which contributes to increasing the severity and morbidity observed in patients. This fact, in turn, may be responsible for economic hardship, particularly in rural populations of developing countries. In the present work, we evaluated the antiophidian properties of 12 Brazilian plant extracts against the hemolytic, coagulant, hemorrhagic and proteolytic effects of...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Snake venom; Lachesis muta; Plant extract; Antivenom; Biological activities.
Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992010000200012
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Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venom J. Venom. Anim. Toxins incl. Trop. Dis.
Barros,LC; Soares,AM; Costa,FL; Rodrigues,VM; Fuly,AL; Giglio,JR; Gallacci,M; Thomazini-Santos,IA; Barraviera,SRCS; Barraviera,B; Ferreira Junior,RS.
Gyroxin, a thrombin-like enzyme isolated from Crotalus durissus terrificus venom and capable of converting fibrinogen into fibrin, presents coagulant and neurotoxic activities. The aim of the present study was to evaluate such coagulant and toxic properties. Gyroxin was isolated using only two chromatographic steps - namely gel filtration (Sephadex G-75) and affinity (Benzamidine Sepharose 6B) - resulting in a sample of high purity, as evaluated by RP-HPLC C2/C18 and electrophoretic analysis that showed a molecular mass of 30 kDa. Gyroxin hydrolyzed specific chromogenic substrates, which caused it to be classified as a serine proteinase and thrombin-like enzyme. It was stable from pH 5.5 to 8.5 and inhibited by Mn²+, Cu²+, PMSF and benzamidine. Human...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Gyroxin; Neurotoxicity; Coagulant activity; Crotalus durissus terrificus; Serine proteinase.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100004
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