Purification,Partial Characterizations,and N‐Terminal Amino Acid Sequence of a Procoagulant Protein FV‐2 from Daboia Russelli Siamensis (Myanmar) Venom |
| |
| Authors: | Weiwei Zhu Zheng Wu Shuhao Shen Jun Liu Nanlin Xiang Yunjian Liao Xi Lin Lixin Chen Qi Chen |
| |
| Institution: | 1. Department of Pharmacology, Medical College, Jinan University, Guangzhou, People's Republic of China;2. Key Laboratory for Regenerative Medicine, Ministry of Education, Jinan University, Guangzhou, People's Republic of China;3. Department of Developmental and Regenerative Biology, Jinan University, Guangzhou, People's Republic of China;4. Department of Physiology, Medical College, Jinan University, Guangzhou, People's Republic of China;5. Department of Pharmacology and Toxicology, Guangdong Institute for Food and Drug Control, Guangdong Province, Guangzhou, People's Republic of China |
| |
| Abstract: | 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 SuperdexTM 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. |
| |
| Keywords: | Snake venom Daboia russelli siamensis procoagulant activity factor X activator N‐terminal sequence |
|
|
