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

Author(s): Jorge H. Petretski, Milton M. Kanashiro, Flavia G. Rodriques, Elias W. Alves, Olga L.T. Machado, Tereza L. Kipnis.

Journal Name: Protein & Peptide Letters

Volume 8 , Issue 3 , 2001


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

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Article Details

Year: 2001
Page: [187 - 192]
Pages: 6
DOI: 10.2174/0929866013409535
Price: $58

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