Purification and characterization of jararassin-I, a thrombin-like enzyme from Bothrops jararaca snake venom
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Data
2004-12-01
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Shanghai Inst Biochemistry, Academia Sinica
Resumo
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 Bbeta chain of fibrinogen while the Aalpha chain and gammachain 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 Bbeta chain of bovine fibrinogen. Single crystals of enzyme were obtained (0.2 mmx0.2 mmx0.2 mm) and used for X-ray diffraction experiments.
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snake venom, Bothrops jararaca, serine protease thrombin-like, fibrinogenolytic activity, crystallization
Como citar
Acta Biochimica Et Biophysica Sinica. Shanghai: Shanghai Inst Biochemistry, Academia Sinica, v. 36, n. 12, p. 798-802, 2004.