Purification and Identification of A 25 KDa Hemorrhagin from B. atrox Venom

Authors: Petretski J.H.; Kanashiro M.M.; Rodriques F.G.; Alves E.W.; Machado O.L.T.; Kipnis T.L.

Source: Protein and Peptide Letters, Volume 8, Number 3, June 2001 , pp. 187-192(6)

Publisher: Bentham Science Publishers

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Abstract:

Viperine and crotaline snake venoms contain one or more hemorrhagic metalloproteinases called hemorrhagins. The most potent hemorrhagins belong to P-III class and have, in adition to the protease domain, a disintegrin-like and a cysteine-rich domains. Although proteolytic degradation of vascular endothelium basement membrane has been established to be the main factor responsible for hemorrhage, several studies reveal other factors that actually do facilitate this process. In this study we report the identification of an P-I class hemorrhagin from Bothrops atrox venom. We have formerly purified an P-III class hemorrhagin from the same venom. Although exhibiting a higher proteolytic activity, the P-I class hemorrhagin showed to be a less efficient hemorrhagin when compared in vivo with the previously described P-III class metalloprotease.

Keywords: HEMORRHAGIN; hemorrhagins; P-III class; Bothrops atrox; P-III class metalloprotease

Language: English

Document Type: Review article

DOI: 10.2174/0929866013409535

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