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The effect of several drugs on the edema-forming activity of Bothrops asper venom was studied plethysmographically using the mouse foot pad assay. Bothrops asper venom induced a dose-dependent edema which developed rapidly and peaked 1 hr after envenomation. Incubation of venom with EDTA before injection resulted in a significant reduction of edema. In(More)
The biochemical characteristics of hemorrhagic metalloproteinases isolated from snake venoms are reviewed, together with their role in the pathogenesis of the local tissue damage characteristic of crotaline and viperine snake envenomations. Venom metalloproteinases differ in their domain structure. Some enzymes comprise only the metalloproteinase domain,(More)
Venoms from eight Bothrops spp. were fractionated by ion-exchange chromatography on CM-Sepharose at pH 8.0 for the purification of myotoxins. Chromatographic profiles showed differences regarding myotoxic components among these venoms. B. alternatus, B. atrox and B. jararaca venoms did not show the major basic myotoxic fractions identified in the other(More)
Local tissue damage induced by crotaline snake venoms includes edema, myonecrosis, hemorrhage, and an inflammatory response associated with a prominent cellular infiltrate. The role of neutrophils in the local tissue damage induced by Bothrops asper snake venom and by myotoxin I, a phospholipase A2 isolated from this venom, was investigated. Male Swiss mice(More)
Venoms from snakes of the genus Bothrops cause pronounced local effects in the victims. These alterations result not only from the direct toxic action of venom components, but also from the prominent inflammatory reaction associated with these envenomations. In this study we investigated the ability of Bothrops asper (BaV) and Bothrops jararaca (BjV) venoms(More)
Several myotoxins have been isolated from Bothrops snake venoms during the last 10 years. All of them are group II basic phospholipases A2, although some lack enzymatic activity (i.e. Lys-49 variants). These myotoxins appear as an antigenically related family of proteins occurring in many, but not all, Bothrops venoms, bearing a close structural and(More)
Zinc-dependent metalloproteinases are responsible for the hemorrhagic activity characteristic of viperid snake venoms. Snake venom metalloproteinases (SVMPs) are classified in various groups (P-I-IV), according to their domain composition. P-III SVMPs, comprising metalloproteinase, disintegrin-like and cysteine-rich domains, exert more potent hemorrhagic(More)
Envenomations by the snake Bothrops asper are characterized by prominent local tissue damage (i.e. myonecrosis), blistering, hemorrhage and edema. Various phospholipases A2 and metalloproteinases that induce local pathological alterations have been purified from this venom. Since these toxins induce a conspicuous inflammatory response, it has been(More)
E nvenoming resulting from snake bites is an important public health hazard in many regions, particularly in tropical and subtropical countries [1–3]. Although antivenoms are being produced by various laboratories in every continent, the burden of snake bite envenoming— causing both morbidity and mortality—still has a great impact on the population and on(More)
A new muscle damaging toxin, myotoxin II, was purified from the venom of Bothrops asper by ion-exchange chromatography on CM-Sephadex C-25. The toxin is a dimeric, basic protein with a monomer mol.wt of 13,341, according to the amino acid composition, and 16,000 on the basis of SDS-polyacrylamide gel electrophoretic mobility. It has a high number of(More)