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A coagulant enzyme from Bothrops brazili snake venom called thrombin-like enzyme was purified by three successive chromatographic steps on Sephadex G-75, DEAE Sephadex A-50 and Sephadex G-50 using 0.05M Tris-HCl buffer pH 8.5. The enzyme was purified 15.9 times with a yield of 28.6% and by PAGE-SDS a single protein band of 48 kDa was obtained both in reducing and non-reducing conditions using 2β-Mercaptoethano., It is a unicatenary a Laboratorio de Biología Molecular, Facultad de Ciencias Biológicas. UNMSM. *luiz27@outlook.com.pe Luis Ruiz, Dan Vivas-Ruiz, Fanny Lazo, Wolfram Seifert, Edith Rodríguez, Gustavo Sandoval... 464 Rev Soc Quím Perú. 83(4) 2017 protein with coagulant activity on both citrated human plasma and bovine fibrinogen. The enzyme showed amidolytic activity on the chromogenic substrate Benzoyl-Arginyl-pNitroaniline (BApNA) and the coagulant potency on bovine fibrinogen was calculated on 121 NIH units of thrombin / mg. The enzyme was inhibited by PMSF and the soybean trypsin inhibitor, therefore, it is a serine protease; the optimum pH for the amidolytic activity was 8.5 and the protein was stable to heat treatment only up to 40 °C. The minimal defibrinogenating dose was 8 μg / g of mouse and by double immunodiffusion tests immunoreactivity was observed with respect to INS polyvalent antibothropic serum.

PURIFICACIÓN Y CARACTERIZACIÓN BIOQUÍMICA DE LA ENZIMA SIMILAR A TROMBINA DEL VENENO DE LA SERPIENTE Bothrops brazili