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  • Title: Purification and characterization of jararassin-I, A thrombin-like enzyme from Bothrops jararaca snake venom.
    Author: Vieira DF, Watanabe L, Sant'ana CD, Marcussi S, Sampaio SV, Soares AM, Arni RK.
    Journal: Acta Biochim Biophys Sin (Shanghai); 2004 Dec; 36(12):798-802. PubMed ID: 15592646.
    Abstract:
    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 Bb chain of fibrinogen while the Aa chain and g 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 Bb chain of bovine fibrinogen. Single crystals of enzyme were obtained (0.2 mm x 0.2 mm x 0.2 mm) and used for X-ray diffraction experiments.
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