Snake Antivenoms: Heterologous and Polyclonal Antisera

References

• Angulo Y., Estrada R., Gutierrez J. M. Clinical and laboratory alterations in horses during immunization with snake venoms for the production of polyvalent (Crotalinae) antivenom. Toxicon 1997; 35: 81–90
   PubMed Web of Science ®Google Scholar
• Aung W., Pakmanee N., Khow O., Nambut C., Sitprija V. Cross neutralization of the lethal activities of Myanmar and Thai Russell's viper venoms by Thai and Myanmar antivenoms. J. Nat. Toxins 2001; 10: 335–342
   PubMedGoogle Scholar
• Carroll S. B., Thalley B. S., Theakston R.D. G., Laing G. Comparison of the purity and efficacy of affinity purified avian antivenoms with commercial equine crotalid antivenoms. Toxicon 1992; 30: 1017–1025
   PubMed Web of Science ®Google Scholar
• Chanutin A., Curnish R. R. The precipitation of plasma proteins by short chain fatty acids. Arch. Biochem. Biophys. 1960; 89: 218–220
   PubMed Web of Science ®Google Scholar
• Chippaux J. P., Goyffon M. Venoms, antivenoms and immunotherapy. Toxicon 1998; 36: 823–846
   PubMed Web of Science ®Google Scholar
• Consroe P., Egen N. B., Russell F. E., Gerrish K., Smith D. C., Sidki A., Landon J. T. Comparison of a new ovine antigen binding fragment (Fab) antivenin for United States Crotalidae with the commercial antivenin for protection against venom‐induced lethality in mice. Am. J. Trop. Med. Hyg. 1995; 53: 507–510
   PubMed Web of Science ®Google Scholar
• Da Silva M. H., Bier O. G. Titration of antiserum to South American rattlesnake (Crotalus durissus terrificus) venom by measuring inhibition of phospholipase A2 activity. Toxicon 1982; 20: 563–569
   PubMed Web of Science ®Google Scholar
• Davis B. D., Kabat E. A., Harris A., Moore D. H. The anticomplementary activity of serum gamma globulin. J. Immunol. 1944; 49: 223–233
   Google Scholar
• dos Santos M. C., Imperio Lima M.R. D., Furtado G. C., Colletto G.M.D. D., Kipnis T. L., Dias da Silva W. Purification of F(ab′)2 anti‐snake venom by caprylic acid: a fast method for obtaining IgG fragments with high neutralization activity, purity and yield. Toxicon 1989; 27: 297–303
   PubMed Web of Science ®Google Scholar
• Elgert K. D. Immunology: Understanding the Immune System. Wiley‐Liss, Inc., New York 1996, pp. 46–57; 269–290
   Google Scholar
• Freifelder D. Physical biochemistry. Applications to Biochemistry and Molecular Biology. W.H. Freeman and Company, New York 1982; 216–322
   Google Scholar
• Freitas T. V., Frezard F. Encapsulation of native crotoxin in liposomes: a safe approach for the production of antivenom and vaccination against Crotalus durissus terrificus venom. Toxicon 1997; 35: 91–100
   PubMed Web of Science ®Google Scholar
• Grandgeorge M., Veron J. L., Lutsch C., Makula M. F., Riffard P., Pepin S., Scherrmann J. M. Preparation of improved F(ab′)2 antivenoms. An example: new polyvalent European viper antivenom (equine). Envenomings and Their Treatments, C. Bon, M. Goyffon. Fondation Marcel Merieux, Lyon 1996; 161–172
   Google Scholar
• Gronski P., Seiler F. R., Schwick H. G. Discovery of antitoxins and development of antibody preparations for clinical uses from 1890 to 1990. Mol. Immunol. 1991; 28: 1321–1332
   PubMed Web of Science ®Google Scholar
• Gutierrez J. M., Avila C., Rojas E., Cerdas L. An alternative in vitro method for testing the potency of the polyvalent antivenom produced in Costa Rica. Toxicon 1988; 26: 411–413
   PubMed Web of Science ®Google Scholar
• Hanlon C. A., Niezgoda M., Morrill P. A., Rupprecht C. E. The incurable wound revisited. Vaccine 2001; 19: 2273–2279
   PubMed Web of Science ®Google Scholar
• Jimenez‐Porras J. M. Intraspecific variations in composition of venom of the jumping viper, Bothrops nummifera. Toxicon 1964; 2: 187
   PubMedGoogle Scholar
• Jimenez‐Porras J. M. Venom proteins of the fer‐de‐lance, Bothrops atrox, from Costa Rica. Toxicon 1964; 2: 155
   PubMedGoogle Scholar
• Karlson‐Stiber C., Persson H., Heath A., Smith D., Al‐Abdulla I. H., Sjostrom L. First clinical experiences with specific sheep Fab fragments in snake bite. Report of a multicentre study of Vipera berus envenoming. J. Int. Med. 1997; 241: 53–58
   PubMed Web of Science ®Google Scholar
• Krifi M. N., El Ayeb M., Dellagi K. The improvement and standardization of antivenom production in developing countries: comparing antivenom quality, therapeutical efficiency and cost. J. Venom. Anim. Toxins 1999; 5: 128–141
   Google Scholar
• Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685
   PubMed Web of Science ®Google Scholar
• Leon G., Valverde J. M., Rojas G., Lomonte B., Gutierrez J. M. Comparative study on the ability of IgG and Fab sheep antivenoms to neutralize local hemorrhage, edema and myonecrosis induced by Bothrops asper (terciopelo) snake venom. Toxicon 2000; 38: 233–244
   PubMed Web of Science ®Google Scholar
• Lomonte B., Leon G., Hanson L. A. Similar effectiveness of Fab and F(ab′)2 antivenoms in the neutralization of hemorrhagic activity of Vipera berus snake venom in mice. Toxicon 1996; 34: 1197–1202
   PubMed Web of Science ®Google Scholar
• Meyer W. P., Habib A. G., Onayade A. A., Yakubu A., Smith D. C., Nasidi A., Daudu I. J., Warrell D. A., Theakston R.D. G. First clinical experiences with a new ovine Fab Echis ocellatus snake bite antivenom in Nigeria: randomized comparative trial with Institute Pasteur Serum (IPSER) Africa antivenom. Am. J. Trop. Med. Hyg. 1997; 56: 291–300
   PubMed Web of Science ®Google Scholar
• Morais J. F., de Freitas M.C. W., Yamaguchi I. K., dos Santos M. C., Dias da Silva W. Snake antivenoms from hyperimmunized horses: comparison of the antivenom activity and biological properties of their whole IgG and F(ab′)2 fragments. Toxicon 1994; 32: 725–734
   PubMed Web of Science ®Google Scholar
• Moroz C., Grotto L., Goldblum N., de Vries A. Enhancement of immunogenicity of snake venom neurotoxins. Animal Toxins, F. E. Russell, P. R. Saunders. Animal Toxins, Pergamon Press, Oxford 1966; 299–302
   Google Scholar
• Otero R., Gutierrez J. M., Rojas G., Nunez V., Diaz A., Miranda E., Uribe A. F., Silva J. F., Ospina J. G., Medina Y., Toro M. F., Garcia M. E., Leon G., Garcia M., Lizano S., De La Torre J., Marquez J., Mena Y., Gonzalez N., Arenas L. C., Puzon A., Blanco N., Sierra A., Espinal M. E., Arboleda M., Jimenez J. C., Ramirez P., Diaz M., Guzman M. C., Barros J., Henao S., Ramirez A., Macea U., Lozano R. A randomized blinded clinical trial of two antivenoms, prepared by caprylic acid or ammonium sulphate fractionation of IgG, in Bothrops and Porthidium snake bites in Colombia: correlation between safety and biochemical characteristics of antivenoms. Toxicon 1999; 37: 895–908
   PubMed Web of Science ®Google Scholar
• Pope C. G. Disaggregation of proteins by enzymes. Br. J. Exp. Pathol. 1938; 19: 245–251
   Google Scholar
• Progress in the Characterization of Venoms and Standardization of Antivenoms. WHO Offset Publication No. 58, Geneva 1981; 9–10
   Google Scholar
• Rojas G., Espinoza M., Lomonte B., Gutierrez J. M. Effect of storage temperature on the stability of the liquid polyvalent antivenom produced in Costa Rica. Toxicon 1990; 28: 101–105
   PubMed Web of Science ®Google Scholar
• Rojas G., Vargas M., Robles A., Gutierrez J. M. Turbidity of hyperimmune equine antivenom: the role of phenol and serum lipoproteins. Toxicon 1993; 31: 61–66
   PubMed Web of Science ®Google Scholar
• Rojas G., Jimenez J. M., Gutierrez J. M. Caprylic acid fractionation of hyperimmune horse plasma: description of a simple procedure for antivenom production. Toxicon 1994; 32: 351–363
   PubMed Web of Science ®Google Scholar
• Smith E. L., Hill R. L., Lehman I. R., Lefkowitz R. J., Handler P., White A. Principles of Biochemistry: General Aspects. McGraw‐Hill International Book Company, Tokyo 1983; 161–174
   Google Scholar
• Smith D. C., Reddi K. R., Laing G., Theakston R.D. G., Landon J. An affinity purified ovine antivenom for the treatment of Vipera berus envenoming. Toxicon 1992; 30: 865–871
   PubMed Web of Science ®Google Scholar
• Steinbuch M., Audran R. The isolation of IgG from mammalian sera with the aid of caprylic acid. Arch. Biochem. Biophys. 1969; 134: 279–284
   PubMed Web of Science ®Google Scholar
• Taranta A., Franklin E. C. Complement fixation by antibody fragments. Science 1961; 134: 1981–1982
   PubMed Web of Science ®Google Scholar
• Theakston R.D. G., Jane Lloy‐Jones M., Reid H. A. Micro‐elisa for detecting and assaying snake venom and venom‐antibody. Lancet 1977; 24: 639–641, Sept.
   Google Scholar
• Theakston R.D. G., Warrell D. A. Antivenoms: a list of hyperimmune sera currently available for the treatment of envenoming by bites and stings. Toxicon 1991; 29: 1419–1470
   PubMed Web of Science ®Google Scholar
• Tijssen P. Practice and Theory of Enzyme Immunoassays. Laboratory Techniques in Biochemistry and Molecular Biology, R. H. Burdon, P. H. van Knippenberg. Elsevier, Amsterdam 1985, pp. 39–59; 95–120
   Google Scholar
• Wilde H. What are today's orphaned vaccines. Clin. Infect. Dis. 2001; 33: 648–650
   PubMed Web of Science ®Google Scholar
• Wilde H., Thipkong P., Sitprija V., Chaiyabutr N. Heterologous antisera and antivenins are essential biologicals. Perspectives on a worldwide crisis. Ann. Intern. Med. 1996; 125: 233–236
   PubMed Web of Science ®Google Scholar