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Pathological changes induced by BaH1, a hemorrhagic proteinase isolated from Bothrops asper (Terciopelo) snake venom, on mouse capillary blood vessels
(1994-08)
The pathological changes induced in capillaries by BaH1, a hemorrhagic metalloproteinase isolated from the venom of Bothrops asper, were studied after i.m. injection in mouse gastrocnemius. Hemorrhage was observed ...
Inhibition of toxic activities of Bothrops asper venom and other crotalid snake venoms by a novel neutralizing mixture
(1997-12)
The majority of snake bites in Central America are caused by Bothrops asper, whose venom induce complex local effects such as myonecrosis, edema and especially hemorrhage. These effects are only partially neutralized by ...
Inhibition by CaNa2EDTA of local tissue damage induced by Bothrops asper (terciopelo) venom: Application in horse immunization for antivenom production
(1998-03-26)
The ability of the chelating agent CaNa2EDTA to inhibit local tissue damage induced by Bothrops asper venom was studied in mice and in horses used for polyvalent (Crotalinae) antivenom production. CaNa2EDTA was devoid of ...
Activity of hemorrhagic metalloproteinase BaH-1 and myotoxin II from Bothrops asper snake venom on capillary endothelial cells in vitro
(1994-04)
In vivo, hemorrhagic toxins isolated from snake venoms cause a disorganization of the basal lamina of capillaries, with a concomitant degenerative process of endothelial cells. In this study we investigated the effects of ...
Skeletal Muscle Necrosis and Regeneration after Injection of BaH1, A Hemorrhagic Metalloproteinase Isolated from the Venom of the Snake Bothrops asper (Terciopelo)
(1995-02)
The effects of BaH1, a hemorrhagic metalloproteinase isolated from Bothrops asper venom, on mouse gastrocnemius muscle was investigated. The toxin induced severe hemorrhage within minutes after injection. Groups of necrotic ...
Inhibition of local hemorrhage and dermonecrosis induced by Bothrops asper snake venom: effectiveness of early in situ administration of the peptidomimetic metalloproteinase inhibitor batimastat and the chelating agent CaNa2EDTA
(2000-11)
The effectiveness of the chelating agent CaNa2EDTA and the peptidomimetic matrix metalloproteinase inhibitor batimastat (BB-94) to inhibit local tissue damage induced by Bothrops asper snake venom was studied in mice. Both ...
Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper (terciopelo)
(1995-01)
A metalloproteinase, named BaP1, was purified to homogeneity from the venom of Bothrops asper (Pacific region) of Costa Rica by ion-exchange chromatography on CM-Sephadex and gel filtration on Sephacryl S-200. The enzyme ...
In vitro activity of BaH1, the main hemorrhagic toxin of Bothrops asper snake venom on bovine endothelial cells
(1995-10)
Incubation of BaH1, the main hemorrhagic toxin purified from the venom of Bothrops asper, with endothelial cells caused the appearance of spaces among the cells. This effect became more noticeable with increasing hemorrhagin ...
Inhibition of the hemorrhagic activity of Bothrops asper venom by a novel neutralizing mixture
(1997-06)
This study screened 25 sera, 19 synthetic products and five antivenoms obtained after immunization for their ability to neutralize the hemorrhagic activity of venom from the snake Bothrops asper. Among the sera screened, ...
Immunological studies on BaH1 and BaPI, two hemorrhagic metalloproteinases from the venom of the snake Bothrops asper
(1995-08)
No immunological cross-reactivity was observed between BaH1 and BaP1, two hemorrhagic metalloproteinases isolated from B. asper venom, by gel immunodiffusion, Western blotting and neutralization studies. Cross-reactivity ...