Purification and partial characterizations of coagulant protein Fla from Daboia russelli siamensis （Myanmar） venom

• Published in: Acta pharmacologica Sinica Vol. 28; no. 10; pp. 1580 - 1584
• Main Author: Huan-huan SUN Qi CHEN Xi LIN Jia-shu CHEN Peng-xin QIU Guang-mei YAN
• Format: Journal Article
• Language: English
• Published: 2007
• Subjects: 治疗方法; 蛇毒液; 血液凝固
• ISSN: 1671-4083; 1745-7254

Aim： To purify and characterize the coagulant protein FIa from Daboia russelli siamensis （Myanmar） venom. Methods： FIa was purified from Daboia russelli siamensis （Myanmar） venom by ion-exchange chromatography on CM-Sephadex C-50, and gel filtration on Sephadex G-75 and a Superdex 75 column. The hemostatic activity of FIa was determined by the method of Williams and Esnouf. The specific chromogenic substrates were used respectively to determine the activation of factor X and prothrombin. The fibrinogen-clotting activity of FIa was determined by the method of Gao et al. Normal saline was used as a negative control while factor Xa and thrombin were used as positive controls, respectively. Results： FIa, a coagulant protein, was achieved by ion-exchange chromatography and gel filtration with a molecular weight of 34 479 and an isoelectric point of 7.2. FIa was shown to have strong hemostatic activity. The hemostatic activity of 0.5 mg FIa was equal to that of 1.5625 u thrombin. FIa primarily activated factor X, however, had no influence on prothrombin, nor did it cleave or clot fibrinogen. Condusion： FIa is a factor X-activating enzyme, which could activate factor X to factor Xa, but has no effect on prothrombin and fibrinogen.