Toxicon, 1993 Three hemorrhagic factors (BaH1, BH2 and BH3) were isolated from the venom of Bothrops asper by gel filtration on Sephacryl S-200, DEAE-Sepharose chromatography, metal chelate affinity chromatography and hydrophobic interaction chromatography. They contain 55% of the total hemorrhagic activity of the whole venom when they are mixed, but lose almost ...
Borkow, Gadi +2 more
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In Silico Molecular Studies of Antiophidic Properties of the Amazonian Tree Cordia nodosa Lam.
Molecules, 2019 We carried out surveys on the use of Cordia nodosa Lam. in the jungles of Bobonaza (Ecuador). We documented this knowledge to prevent its loss under the Framework of the Convention on Biological Diversity and the Nagoya Protocol.
Carmen X. Luzuriaga-Quichimbo +5 more
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SDS-induced hexameric oligomerization of myotoxin-II from Bothrops asper assessed by sedimentation velocity and nuclear magnetic resonance. [PDF]
Eur Biophys J, 2023 Henrickson A +5 more
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The venom of Bothrops asper from Guatemala: toxic activities and neutralization by antivenoms
Toxicon, 2001 Bothrops asper is responsible for approximately half of the snakebite envenomations in Central America. Despite its medical relevance, only the venom of Costa Rican populations of this species has been studied to some detail, and there is very little information on intraspecies variability in venom composition and toxicity. Venom of B.
Saravia Otten, Patricia +8 more
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Iatreia, 2002 En Colombia, el 90-95% de las 3000 mordeduras de serpientes informadas cada año, son ocasionadas por Bothrops spp, con una elevada mortalidad y secuelas.
Mónica Saldarriaga +4 more
doaj
Toxins, 2015 Renealmia alpinia (Rottb.) MAAS, obtained by micropropagation (in vitro) and wild forms have previously been shown to inhibit some toxic activities of Bothrops asper snake venom if preincubated before injection.
Arley Camilo Patiño +5 more
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Inhibitory Effects of Varespladib, CP471474, and Their Potential Synergistic Activity on Bothrops asper and Crotalus durissus cumanensis Venoms. [PDF]
Molecules, 2022 Quiroz S +5 more
europepmc +1 more source
The amino acid sequence of a myotoxic phospholipase from the venom of Bothrops asper
Archives of Biochemistry and Biophysics, 1990 A myotoxic, basic phospholipase A2 (pI greater than 9.5) with anticoagulant activity has been purified from the venom of Bothrops asper, and its amino acid sequence determined by automated Edman degradation. It is distinct from the B. asper phospholipase A2 known as myotoxin I [Lomonte, B. and Gutierrez, J.
Kaiser, Ivan I. +4 more
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Skeletal muscle fiber hypercontraction induced by Bothrops asper myotoxic phospholipases A2 ex vivo does not involve a direct action on the contractile apparatus. [PDF]
Pflugers Arch, 2023 López-Dávila AJ +11 more
europepmc +1 more source
Biochemistry and toxicology of toxins purified from the venom of the snake Bothrops asper
Toxicon, 2009 The isolation and study of individual snake venom components paves the way for a deeper understanding of the pathophysiology of envenomings--thus potentially contributing to improved therapeutic modalities in the clinical setting--and also opens possibilities for the discovery of novel toxins that might be useful as tools for dissecting cellular and ...
Angulo Ugalde, Yamileth, Lomonte, Bruno
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