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Volumn 1429, Issue 1, 1998, Pages 239-248

Isolation, properties and N-terminal amino acid sequence of a factor V activator from Vipera lebetina (Levantine viper) snake venom

Author keywords

Factor V activator; Glycoprotein; Snake venom; Vipera lebetina

Indexed keywords

BLOOD CLOTTING FACTOR 5; ENZYME ACTIVATOR; VENOM;

EID: 0032436007     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00232-5     Document Type: Article
Times cited : (34)

References (37)
  • 1
    • 0022189629 scopus 로고
    • The influence of snake venom enzymes on blood coagulation
    • F. Kornalik, The influence of snake venom enzymes on blood coagulation, Pharmacol. Ther. 29 (1985) 353-405.
    • (1985) Pharmacol. Ther. , vol.29 , pp. 353-405
    • Kornalik, F.1
  • 2
    • 0002623737 scopus 로고
    • Toxins affecting blood coagulation and fibrinolysis
    • W.T. Shier, D. Mebs (Eds.), Marcel Dekker, New York
    • F. Kornalik, Toxins affecting blood coagulation and fibrinolysis, in: W.T. Shier, D. Mebs (Eds.), Handbook of Toxinology, Marcel Dekker, New York, 1990, pp. 683-759.
    • (1990) Handbook of Toxinology , pp. 683-759
    • Kornalik, F.1
  • 4
    • 0345400193 scopus 로고
    • Blood coagulation
    • A.T. Tu (Ed.), John Wiley and Sons, New York
    • A.T. Tu, Blood coagulation, in: A.T. Tu (Ed.), Venoms. Chemistry and Molecular Biology, John Wiley and Sons, New York, 1977, pp. 329-360.
    • (1977) Venoms. Chemistry and Molecular Biology , pp. 329-360
    • Tu, A.T.1
  • 5
    • 0001982823 scopus 로고
    • Snake venom proteins affecting hemostasis and fibrinolysis
    • K. Stocker (Ed.), CRC Press, Boca Raton, FL
    • K. Stocker, Snake venom proteins affecting hemostasis and fibrinolysis, in: K. Stocker (Ed.), Medical Use of Snake Venom Proteins, CRC Press, Boca Raton, FL, 1990, pp. 97-160.
    • (1990) Medical use of Snake Venom Proteins , pp. 97-160
    • Stocker, K.1
  • 6
    • 0025760647 scopus 로고
    • Inventory of α- and β-fibrinogenases from snake venoms
    • F.S. Markland, Inventory of α- and β-fibrinogenases from snake venoms, Thromb. Haemost. 65 (1991) 438-443.
    • (1991) Thromb. Haemost. , vol.65 , pp. 438-443
    • Markland, F.S.1
  • 7
    • 0026675418 scopus 로고
    • The direct acting α-fibrin(ogen)olytic enzymes from snake venoms
    • J. Siigur, E. Siigur, The direct acting α-fibrin(ogen)olytic enzymes from snake venoms, J. Toxicol. - Toxin Rev. 11 (1992) 91-113.
    • (1992) J. Toxicol. - Toxin Rev. , vol.11 , pp. 91-113
    • Siigur, J.1    Siigur, E.2
  • 8
    • 0026713194 scopus 로고
    • Characterization of snake venom components acting on blood coagulation and platelet function
    • C. Ouyang, C.M. Teng, T.F. Huang, Characterization of snake venom components acting on blood coagulation and platelet function, Toxicon 30 (1992) 945-966.
    • (1992) Toxicon , vol.30 , pp. 945-966
    • Ouyang, C.1    Teng, C.M.2    Huang, T.F.3
  • 9
    • 0020334294 scopus 로고
    • Separation of a bradykinin-releasing enzyme from the proteolytic complex of Levantine viper
    • Russ.
    • E.P. Siigur, J.R. Siigur, A.A. Aaviksaar, V.K. Kibirev, D.M. Fedoryak, Separation of a bradykinin-releasing enzyme from the proteolytic complex of Levantine viper, Biokhimiya (Russ.) 47 (1982) 1730-1737.
    • (1982) Biokhimiya , vol.47 , pp. 1730-1737
    • Siigur, E.P.1    Siigur, J.R.2    Aaviksaar, A.A.3    Kibirev, V.K.4    Fedoryak, D.M.5
  • 10
    • 0025961374 scopus 로고
    • E. Siigur, A. Mähar, J. Siigur, β-Fibrinogenase from the venom of
    • E. Siigur, A. Mähar, J. Siigur, β-Fibrinogenase from the venom of Vipera lebetina, Toxicon 29 (1991) 107-118.
    • (1991) Vipera Lebetina, Toxicon , vol.29 , pp. 107-118
  • 11
    • 0025818718 scopus 로고
    • Purification and characterization of lebetase, a fibrinolytic enzyme from Vipera lebetina (snake) venom
    • E. Siigur, J. Siigur, Purification and characterization of lebetase, a fibrinolytic enzyme from Vipera lebetina (snake) venom, Biochim. Biophys. Acta 1074 (1991) 223-229.
    • (1991) Biochim. Biophys. Acta , vol.1074 , pp. 223-229
    • Siigur, E.1    Siigur, J.2
  • 12
    • 0030570469 scopus 로고    scopus 로고
    • cDNA cloning and deduced amino acid sequence of fibrinolytic enzyme (lebetase) from Vipera lebetina snake venom
    • E. Siigur, A. Aaspõllu, A.T. Tu, J. Siigur, cDNA cloning and deduced amino acid sequence of fibrinolytic enzyme (lebetase) from Vipera lebetina snake venom, Biochem. Biophys. Res. Commun. 224 (1996) 229-236.
    • (1996) Biochem. Biophys. Res. Commun. , vol.224 , pp. 229-236
    • Siigur, E.1    Aaspõllu, A.2    Tu, A.T.3    Siigur, J.4
  • 15
    • 84955541782 scopus 로고
    • Effect of snake venoms on factor V
    • A.T. Tu (Ed.), Reptile Venoms and Toxins, Marcel Dekker, New York
    • W. Kisiel, Effect of snake venoms on factor V, in: A.T. Tu (Ed.), Handbook of Natural Toxins, Vol. 5, Reptile Venoms and Toxins, Marcel Dekker, New York, 1991, pp. 253-264.
    • (1991) Handbook of Natural Toxins , vol.5 , pp. 253-264
    • Kisiel, W.1
  • 16
    • 1542652441 scopus 로고
    • A spectrophotometric determination of trypsin and chymotrypsin
    • G.W. Schwert, Y. Takenaka, A spectrophotometric determination of trypsin and chymotrypsin, Biochim. Biophys. Acta 16 (1955) 570-575.
    • (1955) Biochim. Biophys. Acta , vol.16 , pp. 570-575
    • Schwert, G.W.1    Takenaka, Y.2
  • 18
    • 0000857506 scopus 로고
    • A comparative study of enzyme activities in snake venoms
    • D. Mebs, A comparative study of enzyme activities in snake venoms, Int. J. Biochem. 1 (1970) 335-342.
    • (1970) Int. J. Biochem. , vol.1 , pp. 335-342
    • Mebs, D.1
  • 19
    • 84957363672 scopus 로고
    • A colorimetric method for the determination of the proteolytic activity of duodenal juice
    • J. Charney, R.M. Tomarelli, A colorimetric method for the determination of the proteolytic activity of duodenal juice, J. Biol. Chem. 131 (1947) 501-505.
    • (1947) J. Biol. Chem. , vol.131 , pp. 501-505
    • Charney, J.1    Tomarelli, R.M.2
  • 20
    • 50449151040 scopus 로고
    • The fibrin plate method for estimating of fibrinolytic activity
    • T. Astrup, S. Müllertz, The fibrin plate method for estimating of fibrinolytic activity, Arch. Biochem. Biophys. 40 (1952) 346-351.
    • (1952) Arch. Biochem. Biophys. , vol.40 , pp. 346-351
    • Astrup, T.1    Müllertz, S.2
  • 21
    • 0014249131 scopus 로고
    • Fractionation of Vipera russelli venom by gel filtration I
    • G.D. Dimitrov, R.C. Kankonkar, Fractionation of Vipera russelli venom by gel filtration I, Toxicon 5 (1968) 213-221.
    • (1968) Toxicon , vol.5 , pp. 213-221
    • Dimitrov, G.D.1    Kankonkar, R.C.2
  • 22
    • 0017272559 scopus 로고
    • Coagulant protein of Russell's viper venom
    • L. Lorand (Ed.), Academic Press, New York
    • B.C. Furie, B. Furie, Coagulant protein of Russell's viper venom, in: L. Lorand (Ed.), Methods in Enzymology, Vol. 45, Academic Press, New York, 1976, pp. 191-205.
    • (1976) Methods in Enzymology , vol.45 , pp. 191-205
    • Furie, B.C.1    Furie, B.2
  • 23
    • 0346367328 scopus 로고
    • Aggregation of blood platelets by adenosine diphosphate and its reversal
    • G.V.R. Born, Aggregation of blood platelets by adenosine diphosphate and its reversal, Nature 194 (1962) 927-929.
    • (1962) Nature , vol.194 , pp. 927-929
    • Born, G.V.R.1
  • 25
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • M. Dubois, K.A. Gilles, K.K. Hamilton, P.A. Rebers, F. Smith, Colorimetric method for determination of sugars and related substances, Anal. Chem. 28 (1956) 350-356.
    • (1956) Anal. Chem. , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, K.K.3    Rebers, P.A.4    Smith, F.5
  • 26
    • 77049207568 scopus 로고
    • Determination of serum glycoproteins
    • D. Glick (Ed.), Interscience, New York
    • R.J. Winzler, Determination of serum glycoproteins, in: D. Glick (Ed.), Methods of Biochemical Analysis, Vol. 2, Interscience, New York, 1958, pp. 279-311.
    • (1958) Methods of Biochemical Analysis , vol.2 , pp. 279-311
    • Winzler, R.J.1
  • 27
    • 0015524317 scopus 로고
    • Isoelectric focusing of proteins in polyacrylamide gels
    • O. Vesterberg, Isoelectric focusing of proteins in polyacrylamide gels, Biochim. Biophys. Acta 257 (1972) 11-19.
    • (1972) Biochim. Biophys. Acta , vol.257 , pp. 11-19
    • Vesterberg, O.1
  • 28
    • 0017184124 scopus 로고
    • The activation of factor V by factor Xa or α-chymotrypsin and comparison with thrombin and RVV-V action, an improved factor V isolation procedure
    • C.M. Smith, D.J. Hanahan, The activation of factor V by factor Xa or α-chymotrypsin and comparison with thrombin and RVV-V action, an improved factor V isolation procedure, Biochemistry 15 (1976) 1830-1838.
    • (1976) Biochemistry , vol.15 , pp. 1830-1838
    • Smith, C.M.1    Hanahan, D.J.2
  • 29
    • 0018573970 scopus 로고
    • Molecular properties of the factor V-activating enzyme from Russell's viper venom
    • W. Kisiel, Molecular properties of the factor V-activating enzyme from Russell's viper venom, J. Biol. Chem. 254 (1979) 230-234.
    • (1979) J. Biol. Chem. , vol.254 , pp. 230-234
    • Kisiel, W.1
  • 30
    • 0024270675 scopus 로고
    • The factor V-activating enzyme (RVV-V) from Russell's viper venom. Identification of isoproteins RVV-Vα, Vβ and Vγ and their complete amino acid sequen-ces
    • F. Tokunaga, K. Nagasawa, S. Tamura, T. Miyata, S. Iwanaga, W. Kisiel, The factor V-activating enzyme (RVV-V) from Russell's viper venom. Identification of isoproteins RVV-Vα, Vβ and Vγ and their complete amino acid sequen-ces, J. Biol. Chem. 263 (1988) 17471-17481.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17471-17481
    • Tokunaga, F.1    Nagasawa, K.2    Tamura, S.3    Miyata, T.4    Iwanaga, S.5    Kisiel, W.6
  • 31
    • 0030857042 scopus 로고    scopus 로고
    • Cerastotin, a serine protease from Cerastes cerastes venom, with platelet-aggregating and agglutinating properties
    • N. Marrakchi, R. Barbouche, S. Guermazi, H. Karoni, C. Bon, M. El Ayeb, Cerastotin, a serine protease from Cerastes cerastes venom, with platelet-aggregating and agglutinating properties, Eur. J. Biochem. 247 (1997) 121-128.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 121-128
    • Marrakchi, N.1    Barbouche, R.2    Guermazi, S.3    Karoni, H.4    Bon, C.5    El Ayeb, M.6
  • 32
    • 0024278701 scopus 로고
    • Organization of the gene for batroxobin, a thrombin-like snake venom enzyme. Homology with the trypsin/kallikrein gene family
    • N. Itoh, N. Tanaka, I. Gunakoshi, T. Kawasaki, S. Mihashi, I. Yamashina, Organization of the gene for batroxobin, a thrombin-like snake venom enzyme. Homology with the trypsin/kallikrein gene family, J. Biol. Chem. 263 (1988) 7628-7631.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7628-7631
    • Itoh, N.1    Tanaka, N.2    Gunakoshi, I.3    Kawasaki, T.4    Mihashi, S.5    Yamashina, I.6
  • 33
    • 0023811445 scopus 로고
    • Biochemical and physiological studies on a kallikrein-like enzyme from the venom of Crotalus viridis viridis (prairie rattle snake)
    • Y. Komori, T. Nikai, H. Sugihara, Biochemical and physiological studies on a kallikrein-like enzyme from the venom of Crotalus viridis viridis (prairie rattle snake), Biochim. Biophys. Acta 967 (1988) 92-102.
    • (1988) Biochim. Biophys. Acta , vol.967 , pp. 92-102
    • Komori, Y.1    Nikai, T.2    Sugihara, H.3
  • 34
    • 0029945766 scopus 로고    scopus 로고
    • Purification and partial characterization of a thrombin-like/gyroxin enzyme
    • A.S. Aguiar, C.R. Alves, A. Melgarejo, S. Giovanni-de-Simone, Purification and partial characterization of a thrombin-like/gyroxin enzyme, Toxicon 34 (1996) 555-565.
    • (1996) Toxicon , vol.34 , pp. 555-565
    • Aguiar, A.S.1    Alves, C.R.2    Melgarejo, A.3    Giovanni-De-Simone, S.4
  • 35
    • 0023883275 scopus 로고
    • Amino acid sequence of a coagulant enzyme, flavoxobin, from Trimeresurus flavoviridis venom
    • T.C. Shieh, S. Kawabata, H. Kihara, M. Ohno, S. Iwanaga, Amino acid sequence of a coagulant enzyme, flavoxobin, from Trimeresurus flavoviridis venom, J. Biochem. 103 (1988) 596-605.
    • (1988) J. Biochem. , vol.103 , pp. 596-605
    • Shieh, T.C.1    Kawabata, S.2    Kihara, H.3    Ohno, M.4    Iwanaga, S.5
  • 36
    • 0028899505 scopus 로고
    • A novel plasminogen activator from snake venom. Purification, characterization and molecular cloning
    • Y. Zhang, A. Wisner, Y. Xiong, C. Bon, A novel plasminogen activator from snake venom. Purification, characterization and molecular cloning, J. Biol. Chem. 270 (1995) 10246-10255.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10246-10255
    • Zhang, Y.1    Wisner, A.2    Xiong, Y.3    Bon, C.4
  • 37
    • 0026754715 scopus 로고
    • Activation of bovine factor V by an activator purified from the venom of Naja naja oxiana
    • I. Gerads, G. Tans, L.Y. Yukelson, R.F. Zaal, J. Rosing, Activation of bovine factor V by an activator purified from the venom of Naja naja oxiana, Toxicon 30 (1992) 1065-1079.
    • (1992) Toxicon , vol.30 , pp. 1065-1079
    • Gerads, I.1    Tans, G.2    Yukelson, L.Y.3    Zaal, R.F.4    Rosing, J.5


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