메뉴 건너뛰기




Volumn 36, Issue 5, 1998, Pages 745-758

Purification from Bothrops lanceolatus (Fer de Lance) venom of a fibrino(geno)lytic enzyme with esterolytic activity

Author keywords

[No Author keywords available]

Indexed keywords

SNAKE VENOM;

EID: 0345726054     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(97)00118-9     Document Type: Article
Times cited : (24)

References (41)
  • 1
    • 0017883906 scopus 로고
    • Hemorrhagic toxins from western diamondback rattlesnake (Crotalus atrox) venom: Isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin e
    • Bjarnason, J. B. and Tu, A. T. (1978) Hemorrhagic toxins from western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin e. Biochemistry 17, 3395-3404.
    • (1978) Biochemistry , vol.17 , pp. 3395-3404
    • Bjarnason, J.B.1    Tu, A.T.2
  • 2
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum, H., Beier, H. and Gross, H. J. (1987) Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8, 93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 3
    • 0020575296 scopus 로고
    • Isolation and characterization of the hemorrhagic proteinase from timber rattlesnake venom
    • Civello, D. J., Duong, H. L. and Geren, C. R. (1983) Isolation and characterization of the hemorrhagic proteinase from timber rattlesnake venom. Biochemistry 22, 749-755.
    • (1983) Biochemistry , vol.22 , pp. 749-755
    • Civello, D.J.1    Duong, H.L.2    Geren, C.R.3
  • 5
    • 0001232852 scopus 로고
    • An introduction to polyacrylamide gel electrophoresis
    • eds. B. D. Hames, and D. Rickwood, IRL Press Limited, Oxford
    • Hames, B. D. and Rickwood, D. (1982) An introduction to polyacrylamide gel electrophoresis. In Gel electrophroresis of proteins: a practical approach, eds. B. D. Hames, and D. Rickwood, pp. 2-91. IRL Press Limited, Oxford.
    • (1982) Gel Electrophroresis of Proteins: A Practical Approach , pp. 2-91
    • Hames, B.D.1    Rickwood, D.2
  • 6
    • 0015384891 scopus 로고
    • Determination of protein: A modification of the Lowry method that gives a linear photometric response
    • Hartree, E. F. (1972) Determination of protein: a modification of the Lowry method that gives a linear photometric response. Anal. Biochem. 48, 422-427.
    • (1972) Anal. Biochem. , vol.48 , pp. 422-427
    • Hartree, E.F.1
  • 7
    • 0017258208 scopus 로고
    • The thrombin-like enzyme from Bothrops atrox venom
    • Holleman, W. H. and Weiss, L. J. (1976) The thrombin-like enzyme from Bothrops atrox venom. J. Biol. Chem. 251, 1663-1669.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1663-1669
    • Holleman, W.H.1    Weiss, L.J.2
  • 8
    • 0001243390 scopus 로고
    • A modified spectrophotometric determination of chymotrypsin, trypsin and thrombin
    • Hummel, B. C. W. (1959) A modified spectrophotometric determination of chymotrypsin, trypsin and thrombin. Can. J. Biochem. Physiol. 37, 1393-1397.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 1393-1397
    • Hummel, B.C.W.1
  • 10
    • 0022189629 scopus 로고
    • The influence of snake venom enzymes on blood coagulation
    • Kornalik, F. (1985) The influence of snake venom enzymes on blood coagulation. Pharmacol. Ther. 29, 353-405.
    • (1985) Pharmacol. Ther. , vol.29 , pp. 353-405
    • Kornalik, F.1
  • 11
    • 0000795704 scopus 로고
    • Crystalline soybean trypsin inhibitor II. General properties
    • Kunitz, M. (1946) Crystalline soybean trypsin inhibitor II. General properties. J. Gen. Physiol. 30, 291-310.
    • (1946) J. Gen. Physiol. , vol.30 , pp. 291-310
    • Kunitz, M.1
  • 13
    • 0023516712 scopus 로고
    • 2 activity by a colorimetric assay using a pH indicator
    • 2 activity by a colorimetric assay using a pH indicator. Toxicon 25, 1181-1188.
    • (1987) Toxicon , vol.25 , pp. 1181-1188
    • Lôbo De Araújo, A.1    Radvanyi, F.2
  • 14
    • 0027933653 scopus 로고
    • 2 from Bothrops lanceolatus venom: Purification and molecular, enzymatic and pharmacological properties
    • 2 from Bothrops lanceolatus venom: purification and molecular, enzymatic and pharmacological properties. Toxicon 32, 1069-1081.
    • (1994) Toxicon , vol.32 , pp. 1069-1081
    • Lôbo De Araújo, A.1    Radvanyi, F.2    Bon, C.3
  • 15
    • 0019454868 scopus 로고
    • Purification and partial characterization of a thrombin-like enzyme from the venom of the bushmaster snake, Lachesis muta noctivaga
    • Magalhães, A., De Oliveira, G. J. and Diniz, C. R. (1981) Purification and partial characterization of a thrombin-like enzyme from the venom of the bushmaster snake, Lachesis muta noctivaga. Toxicon 19, 279-294.
    • (1981) Toxicon , vol.19 , pp. 279-294
    • Magalhães, A.1    De Oliveira, G.J.2    Diniz, C.R.3
  • 16
    • 0021343383 scopus 로고
    • Characterization of two hemorrhagic factors isolated from the venom of Bothrops neuwiedi (jararaca pintada)
    • Mandelbaum, F. R., Assakura, M. T. and Reichl, A. P. (1984) Characterization of two hemorrhagic factors isolated from the venom of Bothrops neuwiedi (jararaca pintada). Toxicon 22, 193-206.
    • (1984) Toxicon , vol.22 , pp. 193-206
    • Mandelbaum, F.R.1    Assakura, M.T.2    Reichl, A.P.3
  • 17
    • 0020991693 scopus 로고
    • Rattlesnake venom enzymes that interact with components of the hemostatic system
    • Markland, F. S. (1983) Rattlesnake venom enzymes that interact with components of the hemostatic system. J. Toxicol. Toxin Rev. 2, 119-160.
    • (1983) J. Toxicol. Toxin Rev. , vol.2 , pp. 119-160
    • Markland, F.S.1
  • 18
    • 0015153374 scopus 로고
    • Purification and properties of a thrombin-like enzyme from the venom of Crotalus adamanteus (eastern diamondback rattlesnake)
    • Markland, F. S. and Damus, P. S. (1971) Purification and properties of a thrombin-like enzyme from the venom of Crotalus adamanteus (eastern diamondback rattlesnake). J. Biol. Chem. 246, 6460-6473.
    • (1971) J. Biol. Chem. , vol.246 , pp. 6460-6473
    • Markland, F.S.1    Damus, P.S.2
  • 20
    • 0021135661 scopus 로고
    • Protease activity and lethal toxicity of venoms from some little known rattlesnakes
    • Minton, S. A. and Weinstein, S. A. (1984) Protease activity and lethal toxicity of venoms from some little known rattlesnakes. Toxicon 22, 828-830.
    • (1984) Toxicon , vol.22 , pp. 828-830
    • Minton, S.A.1    Weinstein, S.A.2
  • 21
    • 0021284667 scopus 로고
    • Purification of a proteinase (Ac5-proteinase) and characterization of hemorrhagic toxins from the venom of the hundred-pace snake (Agkistrodon acutus)
    • Mori, N., Nikai, T. and Sugihara, H. (1984) Purification of a proteinase (Ac5-proteinase) and characterization of hemorrhagic toxins from the venom of the hundred-pace snake (Agkistrodon acutus). Toxicon 22, 451-461.
    • (1984) Toxicon , vol.22 , pp. 451-461
    • Mori, N.1    Nikai, T.2    Sugihara, H.3
  • 22
    • 0018799069 scopus 로고
    • Thrombin-like and factor X-activator components of Bothrops venom
    • Nahas, L., Kamiguti, A. S. and Barros, M. A. R. (1979) Thrombin-like and factor X-activator components of Bothrops venom. Thromb. Haemost. 41, 314-328.
    • (1979) Thromb. Haemost. , vol.41 , pp. 314-328
    • Nahas, L.1    Kamiguti, A.S.2    Barros, M.A.R.3
  • 23
    • 0017370581 scopus 로고
    • Enzymochemical studies of snake venoms. II. Purification of lethal protein Ac1-proteinase in the venom of Agkistrodon acutus
    • Nikai, T., Sugihara, H. and Tanaka, T. (1977) Enzymochemical studies of snake venoms. II. Purification of lethal protein Ac1-proteinase in the venom of Agkistrodon acutus. J. Pharm. Soc. Jpn. 97, 507-514.
    • (1977) J. Pharm. Soc. Jpn. , vol.97 , pp. 507-514
    • Nikai, T.1    Sugihara, H.2    Tanaka, T.3
  • 24
    • 0017243179 scopus 로고
    • Ancrod, the coagulation enzyme from Malayan pit viper (Agkistrodon rhodostoma) venom
    • Nolan, C., Hall, L. and Barlow, G. H. (1976) Ancrod, the coagulation enzyme from Malayan pit viper (Agkistrodon rhodostoma) venom. Meth. Enzymol. 45, 205-214.
    • (1976) Meth. Enzymol. , vol.45 , pp. 205-214
    • Nolan, C.1    Hall, L.2    Barlow, G.H.3
  • 25
    • 0017293782 scopus 로고
    • The effects of the purified thrombin-like and anticoagulant principles of Agkistrodon acutus venom on blood coagulation in vivo
    • Ouyang, C. and Teng, C. M. (1976) The effects of the purified thrombin-like and anticoagulant principles of Agkistrodon acutus venom on blood coagulation in vivo. Toxicon 14, 45-49.
    • (1976) Toxicon , vol.14 , pp. 45-49
    • Ouyang, C.1    Teng, C.M.2
  • 26
    • 0018094657 scopus 로고
    • Isolation and characterization of three hemorrhagic factors from the venom of Vipera palaestinae
    • Ovadia, M. (1978) Isolation and characterization of three hemorrhagic factors from the venom of Vipera palaestinae. Toxicon 16, 479-487.
    • (1978) Toxicon , vol.16 , pp. 479-487
    • Ovadia, M.1
  • 27
    • 77957248482 scopus 로고
    • Separation of arginine ester hydrolase of Agkistrodon halys blomhoffi venom into three enzymatic entities: Bradykinin-releasing, clotting and permeability increasing
    • Sato, T., Iwanaga, S., Mizushima, Y. and Suzuki, T. (1965) Separation of arginine ester hydrolase of Agkistrodon halys blomhoffi venom into three enzymatic entities: bradykinin-releasing, clotting and permeability increasing. J. Biochem. 57, 380-391.
    • (1965) J. Biochem. , vol.57 , pp. 380-391
    • Sato, T.1    Iwanaga, S.2    Mizushima, Y.3    Suzuki, T.4
  • 28
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins from 1 to 100 kDa
    • Schagger, H. and Jagow, G. V. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Jagow, G.V.2
  • 29
    • 0023487894 scopus 로고
    • Isolation and characterization of a thrombin-like enzyme from the venom of the snake Bothrops insularis (jararaca ilhoa)
    • Selistre, H. S. and Giglio, J. R. (1987) Isolation and characterization of a thrombin-like enzyme from the venom of the snake Bothrops insularis (jararaca ilhoa). Toxicon 25, 1135-1144.
    • (1987) Toxicon , vol.25 , pp. 1135-1144
    • Selistre, H.S.1    Giglio, J.R.2
  • 30
    • 0025961374 scopus 로고
    • β-Fibrinogenase from the venom of Vipera lebetina
    • Siigur, E., Mahar, A. and Siigur, J. (1991) β-Fibrinogenase from the venom of Vipera lebetina. Toxicon 29, 107-118.
    • (1991) Toxicon , vol.29 , pp. 107-118
    • Siigur, E.1    Mahar, A.2    Siigur, J.3
  • 31
    • 0017242939 scopus 로고
    • The coagulant enzyme from Bothrops atrox venom (batroxobin)
    • Stocker, K. and Barlow, G. H. (1976) The coagulant enzyme from Bothrops atrox venom (batroxobin). Meth. Enzymol. 45, 214-223.
    • (1976) Meth. Enzymol. , vol.45 , pp. 214-223
    • Stocker, K.1    Barlow, G.H.2
  • 32
    • 0016136980 scopus 로고
    • Characterization of the venoms of various Bothrops species by immunoelectrophoresis and reaction with fibrinogen agarose
    • Stocker, K., Christ, W. and Leloup, P. (1974) Characterization of the venoms of various Bothrops species by immunoelectrophoresis and reaction with fibrinogen agarose. Toxicon 12, 415-417.
    • (1974) Toxicon , vol.12 , pp. 415-417
    • Stocker, K.1    Christ, W.2    Leloup, P.3
  • 33
    • 0019489993 scopus 로고
    • Enzymochemical studies on snake venoms. IX. Purification and properties of arginine ester hydrolases (HE-2) in the venom of Trimeresurus mucrosquamatus
    • Sugihara, H., Nikai, T., Nimura, A. and Tanaka, T. (1981) Enzymochemical studies on snake venoms. IX. Purification and properties of arginine ester hydrolases (HE-2) in the venom of Trimeresurus mucrosquamatus. J. Pharm. Soc. Jpn. 101, 153-162.
    • (1981) J. Pharm. Soc. Jpn. , vol.101 , pp. 153-162
    • Sugihara, H.1    Nikai, T.2    Nimura, A.3    Tanaka, T.4
  • 34
    • 85047277689 scopus 로고
    • Enzymochemical studies on snake venoms. III. Purification and properties of arginine esterase which possesses clotting activity in the venom of Agkistrodon acutus
    • Sugihara, H., Nikai, T., Oda, H. and Tanaka, T. (1978) Enzymochemical studies on snake venoms. III. Purification and properties of arginine esterase which possesses clotting activity in the venom of Agkistrodon acutus. J. Pharm. Soc. Jpn. 98, 832-840.
    • (1978) J. Pharm. Soc. Jpn. , vol.98 , pp. 832-840
    • Sugihara, H.1    Nikai, T.2    Oda, H.3    Tanaka, T.4
  • 35
    • 0344777787 scopus 로고
    • Novo meio de reação para testes serológicos de dupla difusão em ágar com antígenos de fitobactérias
    • Sugimori, M. H., Rodrigues Neto, J. and Oliveira, A. R. (1986) Novo meio de reação para testes serológicos de dupla difusão em ágar com antígenos de fitobactérias. Summa Phitopathologica 12, 33.
    • (1986) Summa Phitopathologica , vol.12 , pp. 33
    • Sugimori, M.H.1    Rodrigues Neto, J.2    Oliveira, A.R.3
  • 36
    • 0024578365 scopus 로고
    • Effects of venom proteases on peptide chromogenic substrates and bovine prothrombin
    • Teng, C. M., Wang, J. P., Huang, T. F. and Liau, M. Y. (1989) Effects of venom proteases on peptide chromogenic substrates and bovine prothrombin. Toxicon 27, 161-167.
    • (1989) Toxicon , vol.27 , pp. 161-167
    • Teng, C.M.1    Wang, J.P.2    Huang, T.F.3    Liau, M.Y.4
  • 37
    • 0001406395 scopus 로고    scopus 로고
    • Bothrops lanceolatus bites in Martinique: Clinical aspects and treatment
    • eds. C. Bon and M. Goyffon, Editions Fondation Marcel Mérieux, Lyons
    • Thomas, L., and Tyburn, B. (1996) Bothrops lanceolatus bites in Martinique: Clinical aspects and treatment. In Envenomings and Their Treatments, eds. C. Bon and M. Goyffon, pp. 255-265. Editions Fondation Marcel Mérieux, Lyons.
    • (1996) Envenomings and Their Treatments , pp. 255-265
    • Thomas, L.1    Tyburn, B.2
  • 38
    • 0029035079 scopus 로고
    • Prevention of thromboses in human patients with Bothrops lanceolatus envenoming in Martinique: Failure of anticoagulants and efficacy of a monospecific antivenom
    • Thomas, L., Tyburn, B., Bucher, B., Pecout, F., Ketterle, J., Rieux, D., Smadja, D., Garnier, D. and Plumelle, Y. (1995) Prevention of thromboses in human patients with Bothrops lanceolatus envenoming in Martinique: failure of anticoagulants and efficacy of a monospecific antivenom. Am. J. Trop. Med. Hyg. 52, 419-426.
    • (1995) Am. J. Trop. Med. Hyg. , vol.52 , pp. 419-426
    • Thomas, L.1    Tyburn, B.2    Bucher, B.3    Pecout, F.4    Ketterle, J.5    Rieux, D.6    Smadja, D.7    Garnier, D.8    Plumelle, Y.9
  • 39
    • 43949152581 scopus 로고
    • Troubles de la coagulation et thromboses induites par la morsure de serpent (Bothrops lanceolatus) chez I'homme em Martinique
    • Thomas, L., Tyburn, B., Ketterle, J., Rieux, D., Guarnier, D. and Smadja, D. (1994) Troubles de la coagulation et thromboses induites par la morsure de serpent (Bothrops lanceolatus) chez I'homme em Martinique. Réanim. Urgence 3, 25-30.
    • (1994) Réanim. Urgence , vol.3 , pp. 25-30
    • Thomas, L.1    Tyburn, B.2    Ketterle, J.3    Rieux, D.4    Guarnier, D.5    Smadja, D.6
  • 40
    • 0343399024 scopus 로고
    • Hemorrhagic factors. Hemorrhagic proteases from snake venoms
    • eds. H. Pirkle and F.S. Markland, Marcel Dekker, New York
    • Tu, A. T. (1988) Hemorrhagic factors. Hemorrhagic proteases from snake venoms. In Hemostasis and Animal Venoms, eds. H. Pirkle and F.S. Markland, pp. 425-455. Marcel Dekker, New York.
    • (1988) Hemostasis and Animal Venoms , pp. 425-455
    • Tu, A.T.1
  • 41
    • 0024298861 scopus 로고
    • Purification and biochemical characterization of atroxase, a nonhemorrhagic fibrinolytic protease from western diamondback rattlesnake venom
    • Willis, T. W. and Tu, A. T. (1988) Purification and biochemical characterization of atroxase, a nonhemorrhagic fibrinolytic protease from western diamondback rattlesnake venom. Biochemistry 27, 4769-4777.
    • (1988) Biochemistry , vol.27 , pp. 4769-4777
    • Willis, T.W.1    Tu, A.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.