title: Comparative study of anticoagulant and procoagulant properties of 28 snake venoms from families Elapidae, Viperidae, and purified Russell's  viper venom-factor X activator (RVV-X).
abstract: Snake venoms consist of numerous molecules with diverse biological functions used for capturing prey. Each component of venom has a specific target, and alters the biological function of its target. Once these molecules are identified, characterized, and cloned; they could have medical applications. The activated clotting time (ACT) and clot rate were used for screening procoagulant and anticoagulant properties of 28 snake venoms. Crude venoms from Daboia russellii siamensis, Bothrops asper, Bothrops moojeni, and one Crotalus oreganus helleri from Wrightwood, CA, had procoagulant activity. These venoms induced a significant shortening of the ACT and showed a significant increase in the clot rate when compared to the negative control. Factor X activator activity was also measured in 28 venoms, and D. r. siamensis venom was 5-6 times higher than those of B. asper, B. moojeni, and C. o. helleri from Wrightwood County. Russell's viper venom-factor X activator (RVV-X) was purified from D. r. siamensis venom, and then procoagulant activity was evaluated by the ACT and clot rate. Other venoms, Crotalus atrox and two Naja pallida, had anticoagulant activity. A significant increase in the ACT and a significant decrease in the clot rate were observed after the addition of these venoms; therefore, the venoms were considered to have anticoagulant activity. Venoms from the same species did not always have the same ACT and clot rate profiles, but the profiles were an excellent way to identify procoagulant and anticoagulant activities in snake venoms.
authors.affiliation: Program of Medical Microbiology, Faculty of Graduate School, Chulalongkorn University, Bangkok 10330, Thailand.
authors.forename: Montamas
authors.initials: M
authors.lastname: Suntravat
authors.forename: Issarang
authors.initials: I
authors.lastname: Nuchprayoon
authors.forename: John C
authors.initials: JC
authors.lastname: Pérez
mesh_terms: D000818:Animals; D000925:Anticoagulants / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D001777:Blood Coagulation / Q000187:drug effects*; D002863:Chromogenic Compounds / Q000378:metabolism; D003029:Coagulants / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D004546:Elapid Venoms / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D005170:Factor X / Q000187:drug effects; D006801:Humans; D006868:Hydrolysis / Q000187:drug effects; D008666:Metalloendopeptidases / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D014757:Viper Venoms / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*
chemical_list: D000925:Anticoagulants; D002863:Chromogenic Compounds; D003029:Coagulants; D004546:Elapid Venoms; D014757:Viper Venoms; D005170:Factor X; D008666:Metalloendopeptidases; C476775:factor X activator, Russell's viper