Rs and Elites club, Science Research Branch, Islamic Azad University, Tehran

Rs and Elites club, Science Research Branch, Islamic Azad University, Tehran, Iran. 2Department of Venomous Animals and Antivenom Production, Razi Vaccine and Serum Research Institute, Karaj, Iran. Received: 19 June 2012 Accepted: 29 August 2012 Published: 27 February 2013 References 1. White J: Snake venoms and coagulopathy. Toxicon 2005, 45(8):951?67. 2. Sajevic T, Leonard A, Krizaj I: Haemostatically active proteins in snake venoms. Toxicon 2011, 57(5):627?45. 3. Markland FS: Snake venoms and the hemostatic system. Toxicon 1998, 36(12):1749?800. 4. Bello CA, Hermogenes AL, Magalh s A, Veiga SS, Gremski LH, Richardson M, et al: Isolation and biochemical characterization of a fibrinolytic proteinase from Bothrops leucurus (white-tailed jararaca) snake venom. Biochimie 2-Bromo-1,3-difluoro-4-nitrobenzene 2006, 88(2):189?00. 5. Guti rez JM, Rucavado A, Escalante T, D z C: Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage. Toxicon 2005, 45(8):997?011. 6. Guerranti R, Cortelazzo A, Hope-Onyekwere NS, Furlani E, Cerutti H, Puglia M, et al: In vitro effects of Echis carinatus venom on the human plasma proteome. Proteomics 2010, 10(20):3712?722. 7. Berger M, Pinto A, Guimar s JA: Purification and functional characterization of bothrojaractivase, a prothrombin-activatingSalmanizadeh et al. J Venom Anim Toxins incl Trop 3-Amino-1H-indazole-4-carbonitrile Dis. 2013, 19:3 http://www.jvat.org/content/19/1/Page 8 of8.9.10.11.12.13.14.15.16. 17.18.19.20.21. 22.23.24.25.26.27.28.29.metalloproteinase isolated from Bothrops jararaca snake venom. Toxicon 2008, 51(4):488?01. Petrovan RJ, Govers-Riemslag JW, Nowak G, Hemker HC, Rosing J, Tans G: Purification and characterization of multisquamase, the prothrombin activator present in Echis multisquamatus venom. Thromb Res 1997, 88(3):309?16. Yamada D, Sekiya F, Morita T: Isolation and characterization of carinactivase, a novel prothrombin activator in Echis carinatus venom with a unique catalytic mechanism. J Biol Chem 1996, 271(9):5200?207. Ghorbanpur M, Zare Mirakabadi A, Zokaee F, Zolfagharian H, Rabiei H: Purification and partial characterization of a coagulant serine protease from the venom of the Iranian snake Agkistrodon halys. J Venom Anim Toxins incl Trop Dis 2009, 15(3):411?23. Rizzo F, Papasouliotis K, Crawford E, Dodkin S, Cue S: Measurement of prothrombin time (PT) and activated partial thromboplastin time (APTT) on canine citrated plasma samples following different storage conditions. Res Vet Sci 2008, 85(1):166?70. Garc -Manzano A, Gonz ez-Llaven J, Lemini C, Rubio-P C: Standardization of rat blood clotting tests with reagents used for humans. Proc West Pharmacol Soc 2001, 44:153?55. Assi AA, Nasser H: An in vitro and in vivo study of some biological and biochemical effects of Sistrurus malarius barbouri venom. Toxicology 1999, 137(2):81?4. Masci PP, Whitaker AN, de Jersey J: Purification and characterization of a prothrombin activator from the venom of the Australian brown snake, Pseudonaja textilis textilis. Biochem Int 1988, 17(5):825?35. Serrano SM, Maroun RC: Snake venom serine proteinases: sequence homology vs. substrate specificity, a paradox to be solved. Toxicon 2005, 45(8):1115?132. Kini RM: Serine proteases PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/16505107 affecting blood coagulation and fibrinolysis from snake venoms. Pathophysiol Haemost Thromb 2005, 34(4?):200?04. Meier J, Theakston RD: Approximate LD50 determinations of snake venoms PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/8833965 using eight to ten experimental animals. Toxicon 1986, 24(4):395?01. Rao VS, Joseph JS,.

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