Resumo

MESIA GUEVARA, Marco; LAZO MANRIQUE, Fanny  e  YARLEQUE CHOCAS, Armando. Purification and characterization of a new coagulant principle from the venom of Bothrops pictus peruvian snake. Rev. Soc. Quím. Perú [online]. 2011, vol.77, n.3, pp.182-190. ISSN 1810-634X.

A coagulant protein called trombin like enzyme, was purified from the venom of the Bothrops pictus peruvian snake, using two chromatographic steps: Sephadex G-100 SF and CM Sephadex C-50, equilibrated with 0,05 M ammonium acetate buffer pH 6,0. The enzyme was purified 18 folds with 40,74% of yield and the PAGE-SDS analysis showed an unit protein band with 45,4 kDa and of 54,4 kDa under no reducing and reducing s. Thus it is a single polypeptide chain with at least a S-S bond. The enzyme was capable to clot bovine fibrinogen and attack BApNA chromogenic substrate; being an inhibitor agent as well as PMSF serinoprotease inhibitor. It had a 8,0 as optimum pH on BApNA and it was stable until 50 °C. Mn²⁺ ion (10 mM) was a activator instead.

Palavras-chave : Venom; snake; thrombin like; Bothrops pictus; clot.

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