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Purification, Partial Characterizations, and N‐Terminal Amino Acid Sequence of a Procoagulant Protein FV‐2 from Daboia Russelli Siamensis (Myanmar) Venom
Author(s) -
Zhu Weiwei,
Wu Zheng,
Shen Shuhao,
Liu Jun,
Xiang Nanlin,
Liao Yunjian,
Lin Xi,
Chen Lixin,
Chen Qi
Publication year - 2015
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.21713
Subject(s) - venom , factor x , fibrinogen , sephadex , size exclusion chromatography , snake venom , prothrombinase , chemistry , biochemistry , thrombin , peptide sequence , factor ix , coagulation , microbiology and biotechnology , chromatography , enzyme , biology , medicine , platelet , immunology , gene
In this study, we purified and characterized the procoagulant protein FV‐2 from Daboia russelli siamensis (Myanmar) venom using ion‐exchange chromatography on CM‐Sephadex C‐50 and gel filtration on Superdex TM G‐75 column. The activation of factor X and prothrombin was determined, respectively, by specific chromogenic substrates. The fibrinogen‐clotting activity, thermal stability, and pH stability were also determined. The N‐treminal sequence was determined by the National Center of Biomedical Analysis of China. In the end, FV‐2 was achieved with a molecular weight of 13,608.0 Da. It could activate factor X, but did not affect prothrombin or fibrinogen. The suitable pH was 6.5–7.5, and the suitable temperature ranged from 25 to 60°C. The N‐terminal sequence was Asn‐Phe‐Phe‐Gln‐Phe‐Ala‐Glu‐Met‐Ile‐Val‐Lys‐Met‐Thr‐Gly‐Lys. Taken together, our studies suggest that FV‐2 is a factor X–activating enzyme, which can activate factor X to factor Xa, but it has no effect on prothrombin and fibrinogen.