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Volumn 42, Issue 3, 2003, Pages 239-247

In vitro procoagulant and anticoagulant properties of Naja naja naja venom

Author keywords

Blood clotting; Naja naja naja venom; Platelets; Rheometry

Indexed keywords

CHROMOGENIC SUBSTRATE; FIBRIN; GLASS; PHOSPHOLIPASE A2; SNAKE VENOM; THROMBOPLASTIN;

EID: 0242349156     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(03)00137-5     Document Type: Article
Times cited : (19)

References (36)
  • 1
    • 0017099577 scopus 로고
    • 2 with anticoagulant activity. II. Inhibition of the phosholipid activity in coagulation
    • 2 with anticoagulant activity. II. Inhibition of the phosholipid activity in coagulation. Biochem. Biophys. Acta. 429:1976;839-852.
    • (1976) Biochem. Biophys. Acta , vol.429 , pp. 839-852
    • Boffa, M.C.1    Boffa, G.A.2
  • 3
    • 0017601513 scopus 로고
    • Mass-length ratio of fibrin fibers from gel permeation and light scattering
    • Carr M.E., Shen L.L., Hermans J. Mass-length ratio of fibrin fibers from gel permeation and light scattering. Biopolymers. 16:1977;1-15.
    • (1977) Biopolymers , vol.16 , pp. 1-15
    • Carr, M.E.1    Shen, L.L.2    Hermans, J.3
  • 4
    • 0017910967 scopus 로고
    • Size and density of fibrin fibers from turbidity
    • Carr M.E., Hermans J. Size and density of fibrin fibers from turbidity. Macromolecules. 11:1978;46-50.
    • (1978) Macromolecules , vol.11 , pp. 46-50
    • Carr, M.E.1    Hermans, J.2
  • 5
    • 0036526475 scopus 로고    scopus 로고
    • Delayed, reduced or inhibited thrombin production reduces platelet contractile force and results in weaker clot formation
    • Carr M.E. Jr, Martin E.J., Carr S.L. Delayed, reduced or inhibited thrombin production reduces platelet contractile force and results in weaker clot formation. Blood Coagul. Fibrinolysis. 13:2002;193-197.
    • (2002) Blood Coagul. Fibrinolysis , vol.13 , pp. 193-197
    • Carr M.E., Jr.1    Martin, E.J.2    Carr, S.L.3
  • 6
    • 0027517306 scopus 로고
    • Dusart syndrome: A new concept of the relationship between fibrin clot architecture and fibrin clot degradability: Hypofibrinolysis related to an abnormal clot structure
    • Collet J., Soria J., Mirshahi M., Hirsch M., Dagonnet F.B., Caen J., Soria C. Dusart syndrome: a new concept of the relationship between fibrin clot architecture and fibrin clot degradability: hypofibrinolysis related to an abnormal clot structure. Blood. 82:1993;2462-2469.
    • (1993) Blood , vol.82 , pp. 2462-2469
    • Collet, J.1    Soria, J.2    Mirshahi, M.3    Hirsch, M.4    Dagonnet, F.B.5    Caen, J.6    Soria, C.7
  • 8
    • 0026491075 scopus 로고
    • The effect of fibrin structure on fibrinolysis
    • Gabriel D.A., Muga K., Boothrody E.M. The effect of fibrin structure on fibrinolysis. J. Biol. Chem. 267:1992;24259-24263.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24259-24263
    • Gabriel, D.A.1    Muga, K.2    Boothrody, E.M.3
  • 9
    • 0036942570 scopus 로고    scopus 로고
    • A novel prothrombin activator from the venom of Micropechis ikaheka: Isolation and characterization
    • Gao R., Kini M., Gopalakrishnakone P. A novel prothrombin activator from the venom of Micropechis ikaheka: isolation and characterization. Arch. Biochem. Biophys. 408:2002;87-92.
    • (2002) Arch. Biochem. Biophys. , vol.408 , pp. 87-92
    • Gao, R.1    Kini, M.2    Gopalakrishnakone, P.3
  • 11
    • 85030960852 scopus 로고    scopus 로고
    • Comparative studies with surface plasmon resonance and free oscillation rheolmetry on inhibition of platelets with cytochalasin E and monoclonal antibodies towards GPIIb/IIIa
    • Hansson K.M., Tengvall P., Lundström I., Rånby M., Lindahl T.L. Comparative studies with surface plasmon resonance and free oscillation rheolmetry on inhibition of platelets with cytochalasin E and monoclonal antibodies towards GPIIb/IIIa. Biosens. Bioelectron. 2001.
    • (2001) Biosens. Bioelectron.
    • Hansson, K.M.1    Tengvall, P.2    Lundström, I.3    Rånby, M.4    Lindahl, T.L.5
  • 12
    • 0027980074 scopus 로고
    • 2 purified from Heloderma horridum (beaded lizard) venom
    • 2 purified from Heloderma horridum (beaded lizard) venom. Biochem. Biophys. Acta. 1211:1994;61-68.
    • (1994) Biochem. Biophys. Acta , vol.1211 , pp. 61-68
    • Huang, T.F.1    Chiang, H.S.2
  • 16
    • 0028871913 scopus 로고
    • Isolation and properties of a blood coagulation factor X activator from the venom of king cobra (Ophiophagus hannah)
    • Lee W.-H., Zhang Y., Wang W.-Y., Xiong Y.-L., Gao R. Isolation and properties of a blood coagulation factor X activator from the venom of king cobra (Ophiophagus hannah). Toxicon. 33:1995;1263-1276.
    • (1995) Toxicon , vol.33 , pp. 1263-1276
    • Lee, W.-H.1    Zhang, Y.2    Wang, W.-Y.3    Xiong, Y.-L.4    Gao, R.5
  • 20
    • 0020645310 scopus 로고
    • Factors influencing fibrin gel structure studied by flow measurement
    • Okada M., Blombäck B. Factors influencing fibrin gel structure studied by flow measurement. Ann. NY. Acad. Sci. 408:1983;233-253.
    • (1983) Ann. NY. Acad. Sci. , vol.408 , pp. 233-253
    • Okada, M.1    Blombäck, B.2
  • 21
    • 0005396453 scopus 로고    scopus 로고
    • Iso-citrate is a more gentle anticoagulant than citrate
    • Ramström S., Rånby M., Lindahl T.L. Iso-citrate is a more gentle anticoagulant than citrate. Thromb. Haemost. 82:1999;292-293.
    • (1999) Thromb. Haemost. , vol.82 , pp. 292-293
    • Ramström, S.1    Rånby, M.2    Lindahl, T.L.3
  • 22
    • 0032800910 scopus 로고    scopus 로고
    • Laboratory diagnosis of thrombophilia by endothelial cell modulated coagulation
    • Rånby M., Gustavsson K.M., Lindahl T.L. Laboratory diagnosis of thrombophilia by endothelial cell modulated coagulation. Blood Coagul. Fibrinol. 10:1999;173-179.
    • (1999) Blood Coagul. Fibrinol. , vol.10 , pp. 173-179
    • Rånby, M.1    Gustavsson, K.M.2    Lindahl, T.L.3
  • 23
    • 0242284532 scopus 로고    scopus 로고
    • A prothrombin activator from Pseudonaja textilis venom: Its structural and functional similarity to mammalian coagulation factor Xa-Va complex
    • Rao V.S., Kini R.M., Pseurtarin C. a prothrombin activator from Pseudonaja textilis venom: its structural and functional similarity to mammalian coagulation factor Xa-Va complex. Biochem. J. 369:2002;129-139.
    • (2002) Biochem. J. , vol.369 , pp. 129-139
    • Rao, V.S.1    Kini, R.M.2    Pseurtarin, C.3
  • 24
    • 0242432385 scopus 로고    scopus 로고
    • Group D prothrombin activators from snake venom are structural homologues of mammalian blood coagulation factor Xa
    • Rao V.S., Joseph J.S., Kini R.M. Group D prothrombin activators from snake venom are structural homologues of mammalian blood coagulation factor Xa. Biochem. J. 369:2003;635-642.
    • (2003) Biochem. J. , vol.369 , pp. 635-642
    • Rao, V.S.1    Joseph, J.S.2    Kini, R.M.3
  • 25
    • 0000422079 scopus 로고
    • Cobra Bites
    • Reid H.A. Cobra Bites. Br. Med. J. 2:1964;540.
    • (1964) Br. Med. J. , vol.2 , pp. 540
    • Reid, H.A.1
  • 27
    • 0027127390 scopus 로고
    • 2 inhibitors aristolochic acid and PGBx on A23187-stimulated mobilization of arachidonate in human neutrophils are overcome by diacylglycerol or phorbol ester
    • 2 inhibitors aristolochic acid and PGBx on A23187-stimulated mobilization of arachidonate in human neutrophils are overcome by diacylglycerol or phorbol ester. Biochem. Biophys. Acta. 1126:1992;319-326.
    • (1992) Biochem. Biophys. Acta , vol.1126 , pp. 319-326
    • Rosenthal, M.D.1    Lattanzio, K.S.2    Franson, R.C.3
  • 28
    • 0035049438 scopus 로고    scopus 로고
    • Role of catalytic function in the antiplatelet activity of phospholipase A2 cobra (Naja naja naja) venom
    • Rudrammaji L.M., Machiah, Kantha T.P., Gowda T.V. Role of catalytic function in the antiplatelet activity of phospholipase A2 cobra (Naja naja naja) venom. Mol. Cell Biochem. 219:2001;39-44.
    • (2001) Mol. Cell Biochem. , vol.219 , pp. 39-44
    • Rudrammaji, L.M.1    Machiah2    Kantha, T.P.3    Gowda, T.V.4
  • 29
    • 0025732007 scopus 로고
    • Extensive multiplicity of the miscellaneous type of neurotoxin from the venom of the cobra Naja naja naja and structural characterization of major components
    • Shafqat J., Siddiqi A.R., Zaidi Z.H., Jornvall H. Extensive multiplicity of the miscellaneous type of neurotoxin from the venom of the cobra Naja naja naja and structural characterization of major components. FEBS Lett. 284:1991;70-72.
    • (1991) FEBS Lett. , vol.284 , pp. 70-72
    • Shafqat, J.1    Siddiqi, A.R.2    Zaidi, Z.H.3    Jornvall, H.4
  • 34
    • 0023186213 scopus 로고
    • 2 enzymes from Habu (Trimeresurus flavoviridis) venom and their interaction with the alkaloid aristolochic acid
    • 2 enzymes from Habu (Trimeresurus flavoviridis) venom and their interaction with the alkaloid aristolochic acid. Toxicon. 25:1987;501-515.
    • (1987) Toxicon , vol.25 , pp. 501-515
    • Vishwanath, B.S.1    Kini, R.M.2    Gowda, T.V.3
  • 35
    • 0023516713 scopus 로고
    • 2: Its effect on enzymatic and pathological activities
    • 2: its effect on enzymatic and pathological activities. Toxicon. 25:1987;929-937.
    • (1987) Toxicon , vol.25 , pp. 929-937
    • Vishwanath, B.S.1    Gowda, T.V.2
  • 36
    • 0023476040 scopus 로고
    • 2 from Vipera russelli venom with aristolochic acid: A circular dichroism study
    • 2 from Vipera russelli venom with aristolochic acid: a circular dichroism study. Toxicon. 25:1987;939-946.
    • (1987) Toxicon , vol.25 , pp. 939-946
    • Vishwanath, B.S.1    Rao, A.G.A.2    Gowda, T.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.