Resumo

SANDOVAL, Gustavo A. et al. isolation and partial characterization of a thrombin-like enzyme from bothrops atrox peruvian snake venom "jergón". Rev. Soc. Quím. Perú [online]. 2010, vol.76, n.2, pp.156-164. ISSN 1810-634X.

We have determined some biochemical properties of a thrombin-like enzyme (TLE) isolated from Bothrops atroxperuvian snake venom "jergon". In this concern, TLE was purified until homogeneity using three chromatographical steps: on Sephadex G-75, CM-Sephadex C-50 and Agarose-PAB. Furthermore, molecular weight was determinate by PAGE-SDS and associated carbohydrates by hydrolysis and analysis of hexoses, hexosamines and sialic acid. Then, fibrinocoagulant, amidolytic and sterasic activities were measured on bovine fibrinogen, BApNAand BAEE, respectively.As a result of these analyses, we determined that this enzyme represents 1,7% of total venom and was 25,5-fold purified with a 43,3% yield,using BApNA as substrate. This enzyme had 29,6 kDa, where 14,2% was associated carbohydrates. The TLE of B. atrox produced coagulation of bovine fibrinogen and had enzymatic activity on BAEE and BApNA. In conclusion, we have purified and characterized the main component of B. atrox venom related to its coagulant activity.

Palavras-chave : Bothrops atrox; thrombin-like enzyme; venom; coagulation.

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