Thromb Haemost 1991; 65(05): 627-630
DOI: 10.1055/s-0038-1648201
Scientific and Standardization Committee Communications
Schattauer GmbH Stuttgart

Inventory of Exogenous Prothrombin Activators

For the Subcommittee on Nomenclature of Exogenous Hemostatic Factors of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis
J Rosing
The Cardiovascular Research Institute, Department of Biochemistry, University of Limburg, Maastricht, The Netherlands
,
G Tans
The Cardiovascular Research Institute, Department of Biochemistry, University of Limburg, Maastricht, The Netherlands
› Author Affiliations
Further Information

Publication History

Publication Date:
24 July 2018 (online)

 
  • REFERENCES

  • 1 Schieck A, Komalik F, Habermann E. The prothrombin-activating principle from Echis carinatus venom. I. Preparation and biochemical properties. Naunyn Schmiedebergs Arch Pharmacol 1972 272. 402-416
  • 2 Komalik F, Blomback B. Prothrombin activation induced by Ecarin -a prothrombin converting enzyme from Echis carinatus venom. Thromb Res 1975; 6: 57-63
  • 3 Franza Jr BR, Aronson DL, Finlayson JS. Activation of human prothrombin by a procoagulant fraction from the venom of Echis carinatus. Identification of a high molecular weight intermediate with thrombin activity. J Biol Chem 1975; 250: 7057-7060
  • 4 Morita T, Iwanaga S, Suzuki T. The mechanism of activation of bovine prothrombin by an activator isolated from Echis carinatus venom and characterization of the new active intermediates. J Biochem 1976; 79: 1089-1108
  • 5 Morita T, Iwanaga S. Purification and properties of prothrombin activator from the venom of Echis carinatus. J Biochem 1978; 83: 559-570
  • 6 Rhee M-J, Morris S, Kosow DP. Role of meizothrombin and meizothrombin-(des FI) in the conversion of prothrombin to thrombin by the Echis carinatus venom coagulant. Biochemistry 1982; 21: 3437-3443
  • 7 Morita T, Iwanaga S. Prothrombin activator from Echis carinatus venom. Methods Enzymol 1981; 80: 303-311
  • 8 Briet E, Noyes CM, Roberts HR, Griffith MJ. Cleavage and activation of human prothrombin by Echis carinatus venom. Thromb Res 1982; 27: 591-600
  • 9 Morita T, Iwanaga S, Suzuki T. Activation of bovine prothrombin by an activator isolated from Echis carinatus venom. Thromb Res 1976; 8: 59-65
  • 10 Fortova H, Dyr JE, Vodrazka H, Komalik F. Isolation of the prothrombin-converting enzyme from fibrinogenolytic enzymes of Echis carinatus venom by chromatographic and electrophoretic methods. J Chromatogr 1983; 259: 473-479
  • 11 Denson KWE. Clot-inducing substances present in snake venoms with particular reference to Echis carinatus. Thromb Res 1976; 8: 351-360
  • 12 Nahas L, MacFarlane RG, Denson KWE. A study of the coagulant action of eight snake venoms. Thromb Diath Haemorrh 1964; 12: 355-367
  • 13 Gitter S, Levi G, Kochwa S, DeVries A, Rechnic A, Casper J. Studies on the venom of Echis coloratus. Am J Trop Med Hyd 1960; 9: 391-399
  • 14 Guillin MC, Bezeaud A, Menache D. The mechanism of activation of human prothrombin by an activator isolated from Dispholidus typus venom. Biochim Biophys Acta 1978; 537: 160-168
  • 15 Bradlow BA, Atkinson PM, Gomperts ED, Gaillard MC. Studies on the coagulant effects of boomslang (Dispholidus typus) venom. Clin Lab Haematol 1980; 2: 317-331
  • 16 Morita T, Iwanaga S, Sakai A. A prothrombin activator found in the venom of Rhabdophis tigrinus tigrinus snake (Yamakagashi snake). Thromb Haemostas 1985 54. 312 (Abstr).
  • 17 Morita T, Matsuomoto H, Iwanaga S, Sakai A. A prothrombin activator found in Rhabdophis tigrinus tigrinus (Yamakagashi snake) venom. In: Hemostasis and Animal Venoms Pirkle H, Markland Jr FS. (eds). Marcel Dekker Inc; New York, Basel: 1988: 55-66
  • 18 Kornalik F, Taborska E. Procoagulant and defibrinating potency of the venom gland extract of Thelotornis kirtlandi. Thromb Res 1978; 12: 991-1001
  • 19 Atkinson PM, Bradlow BA, White JAM, Greig HBW, Gaillard MC. Clinical features of twig snake (Thelotornis capensis) envenomation. S Afr Med J 1980; 58: 1007-1011
  • 20 Komalik F, Taborska E, Mebs D. Pharmacological and biochemical properties of a venom gland extract from the snake Thelotornis kirtlandi. Toxicon 1978; 16: 535-542
  • 21 Sakuragawa N, Takahashi K. Coagulation studies on Habu (Trimeresurus okinavensis) venom. In: Hemostasis and Animal Venoms Pirkle H, Markland Jr FS. (eds). Marcel Dekker Inc; New York, Basel: 1988: 515-522
  • 22 Sakuragawa N, Takahashi K. Coagulation studies on Habu snake (Trimeresurus okinavensus) venom. Thromb Haemostas 1985 54. 313 (Abstr).
  • 23 Hofmann H, Bon C. Blood coagulation induced by the venom of Bothrops atrox. 1. Identification, purification, and properties of a prothrombin activator. Biochemistry 1987; 26: 772-780
  • 24 Nahas L, Kamiguti AS, Barros MAR. Thrombin-like and factor X-activator components of Bothrops snake venoms. Thromb Haemostas 1979; 41: 314-328
  • 25 Govers-Riemslag JWP, Knapen MJH, Tans G, Zwaal RFA, Rosing J. Stmctural and functional characterization of a prothrombin activator from the venom of Bothrops neuwiedi. Biochim Biophys Acta 1987; 916: 388-401
  • 26 Jobin F, Esnouf MP. Coagulant activity of tiger snake (Notechis scutatus scutatus) venom. Nature 1966; 211: 873-875
  • 27 Tans G, Govers-Riemslag JWP, van Rijn JLML, Rosing J. Purification and properties of a prothrombin activator from the venom of Notechis scutatus scutatus. J Biol Chem 1985; 260: 9366-9372
  • 28 Herrmann RP, Davey MG, Skidmore PH. The coagulation defect after envenomation by the bite of the dugite (Demansia nuchalis affinis), a Western Australian brown snake. Med J Aust 1972; 2: 183-186
  • 29 Chester A, Crawford GPM. In vitro coagulant properties of venoms from Australian snakes. Toxicon 1982; 20: 501-504
  • 30 Marshall LR, Herrmann RP. Coagulant and anticoagulant actions of Australian snake venoms. Thromb Haemostas 1983; 50: 707-711
  • 31 Speijer H, Govers-Riemslag JWP, Zwaal RFA, Rosing J. Prothrombin activation by an activator from the venom of Oxyuranus scutellatus (Taipan snake). J Biol Chem 1986; 261: 13258-13267
  • 32 Williams V, White J. Purification and properties of a procoagulant from peninsula tiger snake (Notechis ater niger) venom. Toxicon 1989; 27: 773-779
  • 33 Owen WG, Jackson CM. Activation of prothrombin with Oxyuranus scutellatus scutellatus (taipan snake) venom. Thromb Res 1973; 3: 705-714
  • 34 Pirkle H, McIntosh M, Theodor J, Vernon S. Activation of prothrombin with taipan snake venom. Thromb Res 1972; 1: 559-568
  • 35 Walker FJ, Owen WG, Esmon CT. Characterization of the prothrombin activator from the venom of Oxyuranus scutellatus scutellatus (taipan venom). Biochemistry 1980; 19: 1020-1023
  • 1 Masci PP, Whitaker AN, DeJersey J. Purification and characterization of a prothrombin activator from the venom of the Australian brown snake, Pseudonaja textilis textilis. Biochem Int 1988; 17: 825-835
  • 37 Masci PP, Whitaker AN, DeJersey J. Purification and characterization of the prothrombin activator of the common brown snake (Pseudonaja ic.xnhs textilis). Thromb Haemosias 1985 54. 265 (Abstr).
  • 38 Seegers WH, Teng C-M, Novoa E. Preparation of bovine prethrombin 2: use of Acutin and activation with prothrombinase or Ecarin. Thromb Res 1980; 19: 11-20
  • 39 Ouyang C, Hong JS, Teng C-M. Purification and properties of the thrombin-like principle of Agkistrodon acutus venom and its comparison with bovine thrombin. Thromb Diath Haemorrh 1971; 26: 224-234
  • 40 Ouyang C, Hong JS. Inhibition of the thrombin-like principle of Agkistrodon acutus venom by group-specific enzyme inhibitors. Toxicon 1974; 12: 449
  • 41 Ouyang C, Teng C-M, Yang FY, Hong JS. Studies of the coagulant and anticoagulant principles of Formosan crotalid venoms. Toxicon 1976; 14: 415
  • 42 Pirkle H, Markland FS, Theodor I. Thrombin-like enzymes of snake venoms: actions on prothrombin. Thromb Res 1976; 8: 619-627
  • 43 Teng C-M, Wang JP, Huang TF, Liau MY. Effects of venom proteases on peptide chromogenic substrates and bovine prothrombin. Toxicon 1989; 27: 161-167
  • 44 Nolan C, Hall LS, Barlow GH. Ancrod, the coagulating enzyme from Malayan pit viper (Agkistrodon rhodostoma) venom. Methods Enzy-mol 1976; 45: 205-213
  • 5 Hatton MWC. Studies on the coagulant enzyme from Agkistrodon rhodostoma venom. Biochem J 1973; 131: 799-807
  • 46 Pitney WR, Regoeczi E. Inactivation of “Arvin” by plasma proteins. Br J Haematol 1970; 19: 67-81
  • 47 Lollar P, Parker CG, Kajenski PJ, Litwiller RD, Fass DN. Degradation of coagulation proteins by an enzyme from Malayan pit viper (Agkistrodon rhodostoma) venom. Biochemistry 1987; 26: 7627-7636
  • 48 Markland FS, Damus PS. Purification and properties of thrombin-like enzyme from the venom of Crotalus adamanteus (Eastern diamond-back rattlesnake). J Biol Chem 1971; 246: 6460-6473
  • 49 Markland FS, Pirkle H. Thrombin-like enzyme from the venom of Crotalus adamanteus (Eastern diamondback rattlesnake). Thromb Res 1977; 10: 487-92
  • 50 Markland FS, Kettner C, Shaw E, Bajwa SS. The inhibition of crotalase, a thrombin-like venom enzyme, by several peptide chloromethyl ketone derivatives. Biochim Biophys Res Commun 1981; 102: 1302-1309
  • 51 Bajwa SS, Markland FS. A new method for purification of the thrombin-like enzyme from the venom of the Eastern diamondback rattlesnake. Thromb Res 1979; 16: 11-23
  • 52 Hendrix H, Lindhout T, Mertens K, Engels W, Hemker HC. Activation of human prothrombin by stoichiometric levels of staphy-locoagulase. J Biol Chem 1983; 258: 3637-3644
  • 53 Kawabata S, Morita T, Iwanaga S, Igarashi H. Enzymatic properties of staphylothrombin, an active molecular complex formed between staphylocoagulase and human prothrombin. J Biochem Tokyo 1985; 98: 1603-1614
  • 54 Drapeau GR. Role of metalloprotease inactivation of the precursor of Staphylococcal protease. J Bacteriol 1978; 136: 607-613
  • 55 Wegrzynowicz Z, Heczko PB, Drapeau GR, Jeljaszewicz J, Pulverer G. Prothrombin activation by a metalloprotease from Staphylococcus aureus. J Clin Microbiol 1980; 12: 138-139
  • 56 Switalski LM, Schwan O, Smyth CJ, Wadstrom T. Peptocoagulase: clotting factor produced by bovine strains of Peptococcus indolicus. J Clin Microbiol 1978; 7: 361-367
  • 57 Wegrzynowicz Z, Ko HL, Pulverer G, Jeljaszewicz J. The nature of clotting and fibrinolytic activities of Bacteroides melaninogenicus. Zentralbl Bakteriol Parasitenkd Infektionskr Hyg Abt 1 Orig Reihe A 1978; 240: 106-111
  • 58 Pulverer G, Wegrzynowicz Z, Ko HL, Jeljaszewicz J. Prothrombin and plasminogen activators produced by Pseudomonas aeruginosa. Zentralbl Bakteriol Parasitenkd Infektionskr Hyg Abt 1 Orig Reihe A 1980; 247: 112-117