Abstract

BELLIDO, Candy et al. A purification and characterization of high molecular weight hemorrhagin present in the snake venom Bothrops Pictus. Rev. Soc. Quím. Perú [online]. 2016, vol.82, n.2, pp.142-151. ISSN 1810-634X.

A hemorrhagin with metalloprotease activity was purified from the venom of Bothrops pictus snake using Sephadex G-75 molecular gel filtration and DEAE A-50 ionic exchange column. Thus a homogeneus protein entity was obtained with 62 kDa under non reducting conditions. Hemorrhagin is a acid protein, attack both casein and collagen being 0,226 μg as a DHM. Chelating agent such as EDTA as well as 2 ß-mercaptoetanol and DTT produced strong inhibition both caseinolitic and hemorrhagic activities. Optimus pH was 7,5 and heating treatment reduced both activities, At 55 °C recovered activity on casein was 30,4%. On the other hand hemorrhagin is an antigenic entity showed on double immunodiffusion test and was neutralizated fulling with 0,5, 1 and 2 doses of antivenom.

Keywords : Snake; venom; Bothrops pictus; metalloprotease; hemorrhage; proteolytic.

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