Crystallization of bothrombin, a fibrinogen‐converting serine protease isolated from the venom of  Bothrops jararaca | Zendy

Watanabe L. | Zendy; Vieira D. F. | Zendy; Bortoleto R. K. | Zendy; Arni R. K. | Zendy

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Crystallization of bothrombin, a fibrinogen‐converting serine protease isolated from the venom of Bothrops jararaca

Author(s) -

Watanabe L.,

Vieira D. F.,

Bortoleto R. K.,

Arni R. K.

Publication year - 2002

Publication title -

acta crystallographica section d

Language(s) - English

Resource type - Journals

ISSN - 1399-0047

DOI - 10.1107/s0907444902003645

Subject(s) - bothrops jararaca , batroxobin , venom , fibrinogen , serine protease , proteases , trypsin , snake venom , thrombin , chemistry , biochemistry , protease , microbiology and biotechnology , platelet , biology , enzyme , immunology

Bothrombin, a snake‐venom serine protease, specifically cleaves fibrinogen, releasing fibrinopeptide A to form non‐crosslinked soft clots, aggregates platelets in the presence of exogeneous fibrinogen and activates blood coagulation factor VIII. Bothrombin shares high sequence homology with other snake‐venom proteases such as batroxobin (94% identity), but only 30 and 34% identity with human α‐thrombin and trypsin, respectively. Single crystals of bothrombin have been obtained and X‐ray diffraction data have been collected at the Laboratorio Nacional de Luz Sincrotron to a resolution of 2.8 Å. The crystals belong to the space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 94.81, b = 115.68, c = 155.97 Å.

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