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Volumn 141, Issue 1, 2007, Pages 25-35

Analysis of inhibition rate enhancement by covalent linkage of antithrombin to heparin as a potential predictor of reaction mechanism

Author keywords

Anticoagulant; Antithrombin; Coagulation factor; Heparin; Mechanism

Indexed keywords

ANTITHROMBIN; BLOOD CLOTTING FACTOR 11A; BLOOD CLOTTING FACTOR 7A; BLOOD CLOTTING FACTOR 9A; CALCIUM ION; HEPARIN; HEPARINOID; LIPID; PROTEINASE; THROMBIN; THROMBOPLASTIN;

EID: 34147220888     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvm001     Document Type: Article
Times cited : (15)

References (61)
  • 1
    • 0033214353 scopus 로고    scopus 로고
    • Normal thrombin generation
    • Butenas, S., van't Veer, C., and Mann, K.G. (1999) "Normal" thrombin generation. Blood 94, 2169-2178
    • (1999) Blood , vol.94 , pp. 2169-2178
    • Butenas, S.1    van't Veer, C.2    Mann, K.G.3
  • 3
    • 33644809565 scopus 로고    scopus 로고
    • Positive feedbacks of coagulation: Their role in threshold regulation
    • Jesty, J. and Beltrami, E. (2005) Positive feedbacks of coagulation: their role in threshold regulation. Arterioscler. Thromb. Vasc. Biol. 25, 2463-2469
    • (2005) Arterioscler. Thromb. Vasc. Biol , vol.25 , pp. 2463-2469
    • Jesty, J.1    Beltrami, E.2
  • 5
    • 0025788582 scopus 로고
    • Activation of human blood coagulation factor XI independent of factor XII: Factor XI is activated by thrombin and factor XIa in the presence of negatively charged surfaces
    • Naito, K. and Fujikawa, K. (1991) Activation of human blood coagulation factor XI independent of factor XII: factor XI is activated by thrombin and factor XIa in the presence of negatively charged surfaces. J. Biol. Chem. 266, 7353-7358
    • (1991) J. Biol. Chem , vol.266 , pp. 7353-7358
    • Naito, K.1    Fujikawa, K.2
  • 6
    • 0029803878 scopus 로고    scopus 로고
    • Control mechanisms in thrombin generation
    • Ofosu, F.A., Liu, L., and Feedman, J. (1996) Control mechanisms in thrombin generation. Semin. Thromb. Haemost. 22, 303-308
    • (1996) Semin. Thromb. Haemost , vol.22 , pp. 303-308
    • Ofosu, F.A.1    Liu, L.2    Feedman, J.3
  • 7
    • 0023244130 scopus 로고
    • The inhibition of thrombin-dependent positive-feedback reactions is critical to the expression of the anticoagulant effect of heparin
    • Ofosu, F.A., Sie, P., Modi, G.J., Fernandez, F., Buchanan, M.R., Blajchman, M.A., Boneu, B., and Hirsh, J. (1987) The inhibition of thrombin-dependent positive-feedback reactions is critical to the expression of the anticoagulant effect of heparin. Biochem. J. 243, 579-588
    • (1987) Biochem. J , vol.243 , pp. 579-588
    • Ofosu, F.A.1    Sie, P.2    Modi, G.J.3    Fernandez, F.4    Buchanan, M.R.5    Blajchman, M.A.6    Boneu, B.7    Hirsh, J.8
  • 9
    • 0032758605 scopus 로고    scopus 로고
    • New insights into low blood clots: Implications for the use of APTT and PT as coagulation screening tests and in monitoring of anticoagulant therapy
    • Bajaj, S.P. and Joist, J.H. (1999) New insights into low blood clots: implications for the use of APTT and PT as coagulation screening tests and in monitoring of anticoagulant therapy. Semin. Thromb. Hemost. 25, 407-418
    • (1999) Semin. Thromb. Hemost , vol.25 , pp. 407-418
    • Bajaj, S.P.1    Joist, J.H.2
  • 10
    • 0034911688 scopus 로고    scopus 로고
    • Roles of platelets and factor XI in the initiation of blood coagulation by thrombin
    • Walsh, P.N. (2001) Roles of platelets and factor XI in the initiation of blood coagulation by thrombin. Thromb. Haemost. 86, 75-82
    • (2001) Thromb. Haemost , vol.86 , pp. 75-82
    • Walsh, P.N.1
  • 12
    • 13544274283 scopus 로고    scopus 로고
    • Factor Xa stimulates fibroblast procollagen production, proliferation, and calcium signaling via PARI activation
    • Blanc-Brude, O.P., Archer, F., Leoni, P., Derian, C., Bolsover, S., Laurent, G.J., and Cahmbers, R.C. (2005) Factor Xa stimulates fibroblast procollagen production, proliferation, and calcium signaling via PARI activation. Exp. Cell. Res. 304, 16-27
    • (2005) Exp. Cell. Res , vol.304 , pp. 16-27
    • Blanc-Brude, O.P.1    Archer, F.2    Leoni, P.3    Derian, C.4    Bolsover, S.5    Laurent, G.J.6    Cahmbers, R.C.7
  • 13
    • 0027254146 scopus 로고
    • Increased thrombin generation and activity in patients with systemic lupus erythematosus and anticardiolipin antibodies: Evidence for a prothrombotic state
    • Ginsberg, J.S., Demers, C., Brill Edwards, P., Johnston, M., Bona, R., Burrows, R.F., Weitz, J., and Denburg, J.A. (1993) Increased thrombin generation and activity in patients with systemic lupus erythematosus and anticardiolipin antibodies: evidence for a prothrombotic state. Blood 81, 2958-2963
    • (1993) Blood , vol.81 , pp. 2958-2963
    • Ginsberg, J.S.1    Demers, C.2    Brill Edwards, P.3    Johnston, M.4    Bona, R.5    Burrows, R.F.6    Weitz, J.7    Denburg, J.A.8
  • 14
    • 32844471084 scopus 로고    scopus 로고
    • Blood coagulation-dependent inflammation. Coagulation-dependent inflammation and inflammation-dependent thrombosis
    • Strukova, S. (2006) Blood coagulation-dependent inflammation. Coagulation-dependent inflammation and inflammation-dependent thrombosis. Front. Biosci. 11, 59-80
    • (2006) Front. Biosci , vol.11 , pp. 59-80
    • Strukova, S.1
  • 16
    • 0025687942 scopus 로고
    • The 'antiphospholipid syndrome' and the 'lupus 'anticoagulant'
    • Cameron, J.S. and Frampton, G. (1990) The 'antiphospholipid syndrome' and the 'lupus 'anticoagulant'. Pediatr. Nephrol. 4, 663-678
    • (1990) Pediatr. Nephrol , vol.4 , pp. 663-678
    • Cameron, J.S.1    Frampton, G.2
  • 17
    • 29244450161 scopus 로고    scopus 로고
    • Thrombin-activatable factor X re-establishes an intrinsic amplification in tenase-deficient plasmas
    • Louvain-Quintard, V.B., Bianchini, E.P., Calmel-Tareau, C., Tagzirt, M., and Le Bonniec, B.F. (2005) Thrombin-activatable factor X re-establishes an intrinsic amplification in tenase-deficient plasmas. J. Biol. Chem. 280, 41352-41359
    • (2005) J. Biol. Chem , vol.280 , pp. 41352-41359
    • Louvain-Quintard, V.B.1    Bianchini, E.P.2    Calmel-Tareau, C.3    Tagzirt, M.4    Le Bonniec, B.F.5
  • 18
    • 0017167631 scopus 로고
    • Inhibition of activated factor XII by antithrombin-heparin cofactor
    • Stead, N., Kaplan, A.P., and Rosenberg, R.D. (1976) Inhibition of activated factor XII by antithrombin-heparin cofactor. J. Biol. Chem. 251, 6481-6488
    • (1976) J. Biol. Chem , vol.251 , pp. 6481-6488
    • Stead, N.1    Kaplan, A.P.2    Rosenberg, R.D.3
  • 19
    • 0032553436 scopus 로고    scopus 로고
    • Characterization of a heparin binding site on the heavy chain of factor XI
    • Zhao, M., Abdel-Razek, T., Sun, M.F., and Gailani, D. (1998) Characterization of a heparin binding site on the heavy chain of factor XI. J. Biol. Chem. 273, 31153-31159
    • (1998) J. Biol. Chem , vol.273 , pp. 31153-31159
    • Zhao, M.1    Abdel-Razek, T.2    Sun, M.F.3    Gailani, D.4
  • 20
    • 0016703241 scopus 로고
    • Inhibition of human factor IXa by human antithrombin
    • Rosenberg, J.S., McKenna, P.W., and Rosenberg, R.D. (1975) Inhibition of human factor IXa by human antithrombin. J. Biol. Chem. 250, 8883-8888
    • (1975) J. Biol. Chem , vol.250 , pp. 8883-8888
    • Rosenberg, J.S.1    McKenna, P.W.2    Rosenberg, R.D.3
  • 21
    • 0028896007 scopus 로고
    • Mechanism of antithrombin III inhibition of factor VIIa/tissue factor activity on cell surfaces. Comparison with tissue factor pathway inhibitor/factor Xa-induced inhibition of factor VIIa/tissue factor activity
    • Rao, L.V., Nordfang, O., Hoang, A.D., and Pendurthi, U.R. (1995) Mechanism of antithrombin III inhibition of factor VIIa/tissue factor activity on cell surfaces. Comparison with tissue factor pathway inhibitor/factor Xa-induced inhibition of factor VIIa/tissue factor activity. Blood 85, 121-129
    • (1995) Blood , vol.85 , pp. 121-129
    • Rao, L.V.1    Nordfang, O.2    Hoang, A.D.3    Pendurthi, U.R.4
  • 22
    • 0015853889 scopus 로고
    • Anticoagulant action of heparin
    • Damus, P.S., Hicks, M., and Rosenberg, R.D. (1973) Anticoagulant action of heparin. Nature 246, 355-357
    • (1973) Nature , vol.246 , pp. 355-357
    • Damus, P.S.1    Hicks, M.2    Rosenberg, R.D.3
  • 24
    • 0025304942 scopus 로고
    • Heparin: What is it? How does it work?
    • Schwartz, B.S. (1990) Heparin: What is it? How does it work?. Clin. Cardiol. 13, VI12-VI15
    • (1990) Clin. Cardiol , vol.13
    • Schwartz, B.S.1
  • 25
    • 0036872229 scopus 로고    scopus 로고
    • Heparin activates antithrombin anticoagulant function by generating new interaction sites (exosites) for blood clotting proteinases
    • Olson, S.T. and Chuang, Y.J. (2002) Heparin activates antithrombin anticoagulant function by generating new interaction sites (exosites) for blood clotting proteinases. Trends. Cardiovasc. Med. 12, 331-338
    • (2002) Trends. Cardiovasc. Med , vol.12 , pp. 331-338
    • Olson, S.T.1    Chuang, Y.J.2
  • 26
    • 0022977122 scopus 로고
    • Role of ternary complexes, in which heparin binds both antithrombin and proteinase, in the acceleration of the reactions between antithrombin and thrombin or factor Xa
    • Danielsson, A.E., Raub, E., Lindahl, U., and Bjork, I. (1986) Role of ternary complexes, in which heparin binds both antithrombin and proteinase, in the acceleration of the reactions between antithrombin and thrombin or factor Xa. J. Biol. Chem. 261, 15467-15473
    • (1986) J. Biol. Chem , vol.261 , pp. 15467-15473
    • Danielsson, A.E.1    Raub, E.2    Lindahl, U.3    Bjork, I.4
  • 27
    • 0030772454 scopus 로고    scopus 로고
    • Covalent antithrombin-heparin complexes with high anticoagulant activity: Intravenous, subcutaneous and intratracheal administration
    • Chan, A.K., Berry, L., O'Brodovich, H., Klement, P., Mitchell, L., Baranowski, B., Monagle, P., and Andrew, M. (1997) Covalent antithrombin-heparin complexes with high anticoagulant activity: Intravenous, subcutaneous and intratracheal administration. J. Biol. Chem. 272, 22111-22117
    • (1997) J. Biol. Chem , vol.272 , pp. 22111-22117
    • Chan, A.K.1    Berry, L.2    O'Brodovich, H.3    Klement, P.4    Mitchell, L.5    Baranowski, B.6    Monagle, P.7    Andrew, M.8
  • 28
    • 0037047084 scopus 로고    scopus 로고
    • Antithrombin-heparin covalent complex: A possible alternative to heparin for arterial thrombosis prevention
    • Chan, A.K.C., Rak, J., Berry, L.R., Liao, P., Vlasin, M., Weitz, J.I., and Klement, P. (2002) Antithrombin-heparin covalent complex: a possible alternative to heparin for arterial thrombosis prevention. Circulation 106, 261-265
    • (2002) Circulation , vol.106 , pp. 261-265
    • Chan, A.K.C.1    Rak, J.2    Berry, L.R.3    Liao, P.4    Vlasin, M.5    Weitz, J.I.6    Klement, P.7
  • 29
    • 0036215406 scopus 로고    scopus 로고
    • Decreased concentrations of heparinoids are required to inhibit thrombin generation in plasma from newborns and children compared to plasma from adults due to reduced thrombin potential
    • Chan, A.K.C., Berry, L.R., Monagle, P.T., and Andrew, M. (2002) Decreased concentrations of heparinoids are required to inhibit thrombin generation in plasma from newborns and children compared to plasma from adults due to reduced thrombin potential. Thromb. Haemost. 87, 606-613
    • (2002) Thromb. Haemost , vol.87 , pp. 606-613
    • Chan, A.K.C.1    Berry, L.R.2    Monagle, P.T.3    Andrew, M.4
  • 30
    • 0036684179 scopus 로고    scopus 로고
    • Inhibition of fibrin-bound thrombin by a covalent antithrombin-heparin complex
    • Berry, L.R., Becker, D.L., and Chan, A.K. (2002) Inhibition of fibrin-bound thrombin by a covalent antithrombin-heparin complex. J. Biochem. (Tokyo) 132, 167-176
    • (2002) J. Biochem. (Tokyo) , vol.132 , pp. 167-176
    • Berry, L.R.1    Becker, D.L.2    Chan, A.K.3
  • 33
    • 0026690347 scopus 로고
    • Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement
    • Olson, S.T., Bjork, I., Sheffer, R., Craig, P.A., Shore, J.D., and Choay, J. (1992) Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement. J. Biol. Chem. 267, 12528-12538
    • (1992) J. Biol. Chem , vol.267 , pp. 12528-12538
    • Olson, S.T.1    Bjork, I.2    Sheffer, R.3    Craig, P.A.4    Shore, J.D.5    Choay, J.6
  • 34
    • 0027498670 scopus 로고
    • Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin
    • Olson, S.T., Bjork, I., and Shore, J.D. (1993) Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin. Methods Enzymol. 222, 525-559
    • (1993) Methods Enzymol , vol.222 , pp. 525-559
    • Olson, S.T.1    Bjork, I.2    Shore, J.D.3
  • 35
    • 2442458577 scopus 로고    scopus 로고
    • Binding of heparin to plasma proteins and endothelial surfaces is inhibited by covalent linkage to antithrombin
    • Chan, A.K.C., Paredes, N., Thong, B., Chindemi, P., Paes, B., Berry, L.R., and Monagle, P. (2004) Binding of heparin to plasma proteins and endothelial surfaces is inhibited by covalent linkage to antithrombin. Thromb. Haemost. 91, 1009-1018
    • (2004) Thromb. Haemost , vol.91 , pp. 1009-1018
    • Chan, A.K.C.1    Paredes, N.2    Thong, B.3    Chindemi, P.4    Paes, B.5    Berry, L.R.6    Monagle, P.7
  • 36
    • 13244269951 scopus 로고    scopus 로고
    • Latent antithrombin and its detection, formation and turnover in the circulation
    • Mushunje, A., Evans, G., Brennan, S.O., Carrell, R.W., and Zhou, A. (2004) Latent antithrombin and its detection, formation and turnover in the circulation. J. Thromb. Haemost. 2, 2170-2177
    • (2004) J. Thromb. Haemost , vol.2 , pp. 2170-2177
    • Mushunje, A.1    Evans, G.2    Brennan, S.O.3    Carrell, R.W.4    Zhou, A.5
  • 37
    • 0041315481 scopus 로고    scopus 로고
    • Mechanism of catalysis of inhibition of factor IXa by antithrombin in the presence of heparin or pentasaccharide
    • Wiebe, E.M., Stafford, A.R., Fredenburgh, J.C., and Weitz, J.I. (2003) Mechanism of catalysis of inhibition of factor IXa by antithrombin in the presence of heparin or pentasaccharide. J. Biol. Chem. 278, 35767-35774
    • (2003) J. Biol. Chem , vol.278 , pp. 35767-35774
    • Wiebe, E.M.1    Stafford, A.R.2    Fredenburgh, J.C.3    Weitz, J.I.4
  • 38
    • 0842288664 scopus 로고    scopus 로고
    • Separation of latent, prelatent, and native forms of human antithrombin by heparin affinity high-performance liquid chromatography
    • Karlsson, G. and Winge, S. (2004) Separation of latent, prelatent, and native forms of human antithrombin by heparin affinity high-performance liquid chromatography. Protein Expr. Purif. 33, 339-345
    • (2004) Protein Expr. Purif , vol.33 , pp. 339-345
    • Karlsson, G.1    Winge, S.2
  • 39
    • 0016346287 scopus 로고
    • Substrates of Hageman factor I. Isolation and characterization of human factor XI (PTA) and inhibition of the activated enzyme by alpha-1-antitrypsin
    • Heck, L.W. and Kaplan, A.P. (1974) Substrates of Hageman factor I. Isolation and characterization of human factor XI (PTA) and inhibition of the activated enzyme by alpha-1-antitrypsin. J. Exp. Med. 140, 1615-1630
    • (1974) J. Exp. Med , vol.140 , pp. 1615-1630
    • Heck, L.W.1    Kaplan, A.P.2
  • 40
    • 0017740353 scopus 로고
    • Human blood coagulation factor XI. Purification, properties, and mechanism of activation by activated factor XII
    • Bouma, B.N. and Griffin, J.H. (1977) Human blood coagulation factor XI. Purification, properties, and mechanism of activation by activated factor XII. J. Biol. Chem. 252, 6432-6437
    • (1977) J. Biol. Chem , vol.252 , pp. 6432-6437
    • Bouma, B.N.1    Griffin, J.H.2
  • 41
    • 0020314265 scopus 로고
    • Kinetics of the heparin-enhanced antithrombin III/thrombin reaction. Evidence for a template model for the mechanism of action of heparin
    • Griffith, M.J. (1982) Kinetics of the heparin-enhanced antithrombin III/thrombin reaction. Evidence for a template model for the mechanism of action of heparin. J. Biol. Chem. 257, 7360-7365
    • (1982) J. Biol. Chem , vol.257 , pp. 7360-7365
    • Griffith, M.J.1
  • 42
    • 33646929467 scopus 로고    scopus 로고
    • Anticoagulation therapy thromboembolism
    • Cundiff, D.K. (2004) Anticoagulation therapy thromboembolism. Med. Gen. Med. 6, 5
    • (2004) Med. Gen. Med , vol.6 , pp. 5
    • Cundiff, D.K.1
  • 44
    • 0034685780 scopus 로고    scopus 로고
    • The conformational activation of antithrombin. A 2.85-A structure of a fluorescein derivative reveals an electrostatic link between the hinge and heparin binding regions
    • Huntington, J.A., McCoy, A., Belzar, K.J., Pei, X.Y., Gettins, P.G.W., and Carrell, R.W. (2000) The conformational activation of antithrombin. A 2.85-A structure of a fluorescein derivative reveals an electrostatic link between the hinge and heparin binding regions. J. Biol. Chem. 275, 15377-15383
    • (2000) J. Biol. Chem , vol.275 , pp. 15377-15383
    • Huntington, J.A.1    McCoy, A.2    Belzar, K.J.3    Pei, X.Y.4    Gettins, P.G.W.5    Carrell, R.W.6
  • 45
    • 0027163028 scopus 로고
    • Antithrombin III- and heparin cofactor II-mediated anticoagulant and antiprotease actions of heparin and its synthetic analogues
    • Jeske, W. and Fareed, J. (1993) Antithrombin III- and heparin cofactor II-mediated anticoagulant and antiprotease actions of heparin and its synthetic analogues. Semin. Throm. Hemostas. 19, 241-247
    • (1993) Semin. Throm. Hemostas , vol.19 , pp. 241-247
    • Jeske, W.1    Fareed, J.2
  • 46
    • 0033525536 scopus 로고    scopus 로고
    • Exosites 1 and 2 are essential for protection of fibrin-bound thrombin from heparin-catalyzed inhibition by antithrombin and heparin cofactor II
    • Becker, D.L., Fredenburgh, J.C., Stafford, A.R., and Weitz, J.I. (1999) Exosites 1 and 2 are essential for protection of fibrin-bound thrombin from heparin-catalyzed inhibition by antithrombin and heparin cofactor II. J. Biol. Chem. 274, 6226-6233
    • (1999) J. Biol. Chem , vol.274 , pp. 6226-6233
    • Becker, D.L.1    Fredenburgh, J.C.2    Stafford, A.R.3    Weitz, J.I.4
  • 47
    • 0027475222 scopus 로고
    • Complex-dependent inhibition of factor VIIa by antithrombin III and heparin
    • Lawson, J.H., Butenas, S., Ribarik, N., and Mann, K.G. (1993) Complex-dependent inhibition of factor VIIa by antithrombin III and heparin. J. Biol. Chem. 268, 767-770
    • (1993) J. Biol. Chem , vol.268 , pp. 767-770
    • Lawson, J.H.1    Butenas, S.2    Ribarik, N.3    Mann, K.G.4
  • 48
    • 9144269020 scopus 로고    scopus 로고
    • Accelerating ability of synthetic oligosaccharides on antithrombin inhibition of proteinases of the clotting and fibrinolytic systems. Comparison with heparin and low molecular weight heparin
    • Olson, S.T., Swanson, R., Raub-Segall, E., Bedsted, T., Sadri, M., Petitou, M., Herault, J.P., Herbert, J.M., and Bjork, I. (2004) Accelerating ability of synthetic oligosaccharides on antithrombin inhibition of proteinases of the clotting and fibrinolytic systems. Comparison with heparin and low molecular weight heparin. Thromb. Haemost. 92, 929-939
    • (2004) Thromb. Haemost , vol.92 , pp. 929-939
    • Olson, S.T.1    Swanson, R.2    Raub-Segall, E.3    Bedsted, T.4    Sadri, M.5    Petitou, M.6    Herault, J.P.7    Herbert, J.M.8    Bjork, I.9
  • 49
    • 0032497417 scopus 로고    scopus 로고
    • Mechanism of factor IXa inhibition by antithrombin in the presence of unfractionated and low molecular weight heparins and fucoidan
    • Mauray, S., de Raucourt, E., Talbot, J.C., Dachary-Prigent, J., Jozefowicz, M., and Fischer, A.M. (1998) Mechanism of factor IXa inhibition by antithrombin in the presence of unfractionated and low molecular weight heparins and fucoidan. Biochim. Biophys. Acta 1387, 184-194
    • (1998) Biochim. Biophys. Acta , vol.1387 , pp. 184-194
    • Mauray, S.1    de Raucourt, E.2    Talbot, J.C.3    Dachary-Prigent, J.4    Jozefowicz, M.5    Fischer, A.M.6
  • 50
    • 0019499060 scopus 로고
    • The molecular-weight dependence of the rate-enhancing effect of heparin on the inhibition of thrombin, factor Xa, factor IXa, factor XIa, factor XIIa and kallikrein by antithrombin
    • Holmer, E., Kurachi, K., and Soderstrom, G. (1981) The molecular-weight dependence of the rate-enhancing effect of heparin on the inhibition of thrombin, factor Xa, factor IXa, factor XIa, factor XIIa and kallikrein by antithrombin. Biochem. J. 193, 395-400
    • (1981) Biochem. J , vol.193 , pp. 395-400
    • Holmer, E.1    Kurachi, K.2    Soderstrom, G.3
  • 51
    • 0030131068 scopus 로고    scopus 로고
    • Mechanism of thrombin inactivation by immobilized heparin
    • Byun, Y., Jacobs, H.A., and Kim, S.W. (1996) Mechanism of thrombin inactivation by immobilized heparin. J. Biomed. Mater. Res. 30, 423-127
    • (1996) J. Biomed. Mater. Res , vol.30 , pp. 423-127
    • Byun, Y.1    Jacobs, H.A.2    Kim, S.W.3
  • 52
    • 0035954370 scopus 로고    scopus 로고
    • Localization of a heparin binding site in the catalytic domain of factor XIa
    • Badellino, K.O. and Walsh, P.N. (2001) Localization of a heparin binding site in the catalytic domain of factor XIa. Biochemistry 40, 7569-7580
    • (2001) Biochemistry , vol.40 , pp. 7569-7580
    • Badellino, K.O.1    Walsh, P.N.2
  • 53
    • 0007392227 scopus 로고
    • Activation of factor VII bound to tissue factor: A key early step in the tissue factor pathway of blood coagulation
    • Rao, L.V.M. and Rapaport, S.I. (1988) Activation of factor VII bound to tissue factor: A key early step in the tissue factor pathway of blood coagulation. Proc. Natl. Acad. Sci. USA 85, 6687-6691
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6687-6691
    • Rao, L.V.M.1    Rapaport, S.I.2
  • 54
    • 0034720739 scopus 로고    scopus 로고
    • The tissue factor region that interacts with substrates factor IX and factor X
    • Kirchhofer, D., Lipari, M.T., Moran, P., Eigenbrot, C., and Kelley, R.F. (2000) The tissue factor region that interacts with substrates factor IX and factor X. Biochemistry 39, 7380-7387
    • (2000) Biochemistry , vol.39 , pp. 7380-7387
    • Kirchhofer, D.1    Lipari, M.T.2    Moran, P.3    Eigenbrot, C.4    Kelley, R.F.5
  • 55
    • 0027263354 scopus 로고
    • Binding of factor VIIa to tissue factor permits rapid antithrombin III/heparin inhibition of factor VIIa
    • Rao, L.V., Rapaport, S.I., and Hoang, A.D. (1993) Binding of factor VIIa to tissue factor permits rapid antithrombin III/heparin inhibition of factor VIIa. Blood 81, 2600-2607
    • (1993) Blood , vol.81 , pp. 2600-2607
    • Rao, L.V.1    Rapaport, S.I.2    Hoang, A.D.3
  • 56
    • 0031080132 scopus 로고    scopus 로고
    • Determination of the kinetic constants of tissue factor/factor VII/factor VIIa and antithrombin/heparin using surface plasmon resonance
    • Bjorquist, P. and Bostrom, S. (1997) Determination of the kinetic constants of tissue factor/factor VII/factor VIIa and antithrombin/heparin using surface plasmon resonance. Thromb. Res. 85, 225-236
    • (1997) Thromb. Res , vol.85 , pp. 225-236
    • Bjorquist, P.1    Bostrom, S.2
  • 57
    • 33645965879 scopus 로고    scopus 로고
    • Pentasaccharide enhances the inactivation of factor Xa by antithrombin by promoting the assembly of a Michaelis-type intermediate complex. Demonstration by rapid kinetic, surface plasmon resonance, and competitive binding studies
    • Rezaie, A.R. (2006) Pentasaccharide enhances the inactivation of factor Xa by antithrombin by promoting the assembly of a Michaelis-type intermediate complex. Demonstration by rapid kinetic, surface plasmon resonance, and competitive binding studies. Biochemistry 45, 5324-5329
    • (2006) Biochemistry , vol.45 , pp. 5324-5329
    • Rezaie, A.R.1
  • 58
    • 0037931367 scopus 로고    scopus 로고
    • Mechanisms responsible for catalysis of the inhibition of factor Xa or thrombin by antithrombin using a covalent antithrombin-heparin complex
    • Paredes, N., Wang, A., Berry, L.R., Smith, L.J., Stafford, A.R., Weitz, J.I., and Chan, A.K.C. (2003) Mechanisms responsible for catalysis of the inhibition of factor Xa or thrombin by antithrombin using a covalent antithrombin-heparin complex. J. Biol. Chem. 278, 23398-23409
    • (2003) J. Biol. Chem , vol.278 , pp. 23398-23409
    • Paredes, N.1    Wang, A.2    Berry, L.R.3    Smith, L.J.4    Stafford, A.R.5    Weitz, J.I.6    Chan, A.K.C.7
  • 59
    • 0019163952 scopus 로고
    • The kinetics of hemostatic enzyme-antithrombin interactions in the presence of low molecular weight heparin
    • Jordan, R.E., Oosta, G.M., Gardner, W.T., and Rosenberg, R.D. (1980) The kinetics of hemostatic enzyme-antithrombin interactions in the presence of low molecular weight heparin. J. Biol. Chem. 255, 10081-10090
    • (1980) J. Biol. Chem , vol.255 , pp. 10081-10090
    • Jordan, R.E.1    Oosta, G.M.2    Gardner, W.T.3    Rosenberg, R.D.4
  • 60
    • 0020325434 scopus 로고
    • The rate-determining step of the heparin-catalyzed antithrombin/thrombin reaction is independent of thrombin
    • Pletcher, C.H. and Nelsestuen, G.L. (1982) The rate-determining step of the heparin-catalyzed antithrombin/thrombin reaction is independent of thrombin. J. Biol. Chem. 257, 5342-5345
    • (1982) J. Biol. Chem , vol.257 , pp. 5342-5345
    • Pletcher, C.H.1    Nelsestuen, G.L.2
  • 61
    • 0025831251 scopus 로고
    • Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects
    • Olson, S.T. and Bjork, I. (1991) Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects. Biochem. J. 266, 6353-6364
    • (1991) Biochem. J , vol.266 , pp. 6353-6364
    • Olson, S.T.1    Bjork, I.2


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