| 8 | Purification and Characterization of Jararassin-I, A Thrombin-like Enzyme from Bothrops jararaca Snake Venom显示文摘A thrombin-like serine protease, jararassin-I, was isolated from the venom of Bothrops jararaca. The protein was obtained in high yield and purity by a single chromatographic step using the affinity resin Benzamidine-Sepharose CL-6B. SDS-PAGE and dynamic light scattering analyses indicated that the molecular mass of the enzyme was about 30 kD. The enzyme possessed fibrinogenolytic and coagulant activities. The jararassin-I degraded the Bβ chain of fibrinogen while theAα chain and γ chain were unchanged. Proteases inhibitors, PMSF and benzamidine inhibited the coagulant activity. These results showed jararassin- I is a serine protease similar to coagulating thrombin-like snake venom proteases, but it specifically cleaves Bβ chain of bovine fibrinogen. Single crystals of enzyme were obtained (0.2 mm×0.2 mm×0.2 mm) and used for X-ray diffraction experiments. | Débora F. VIEIRA Leandra WATANABE Carolina D. SANT'ANA Silvana MARCUSSI Suely V. SAMPAIO Andreimar M. SOARES Raghuvir K. ARNI | 2004 | Acta Biochimica et Biophysica Sinica2004，36，12： | 1 |
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