메뉴 건너뛰기




Volumn 288, Issue 39, 2013, Pages 27789-27800

Membrane binding by prothrombin mediates its constrained presentation to prothrombinase for cleavage

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE BINDING; PROTHROMBINASE;

EID: 84884738672     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.502005     Document Type: Article
Times cited : (27)

References (54)
  • 1
    • 0025311157 scopus 로고
    • Surface-dependent reactions of the vitamin K-dependent enzyme complexes
    • Mann, K. G., Nesheim, M. E., Church, W. R., Haley, P., and Krishnaswamy, S. (1990) Surface-dependent reactions of the vitamin K-dependent enzyme complexes. Blood 76, 1-16
    • (1990) Blood , vol.76 , pp. 1-16
    • Mann, K.G.1    Nesheim, M.E.2    Church, W.R.3    Haley, P.4    Krishnaswamy, S.5
  • 2
    • 0023924910 scopus 로고
    • Cofactor proteins in the assembly and expression of blood clotting enzyme complexes
    • Mann, K. G., Jenny, R. J., and Krishnaswamy, S. (1988) Cofactor proteins in the assembly and expression of blood clotting enzyme complexes. Annu. Rev. Biochem. 57, 915-956
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 915-956
    • Mann, K.G.1    Jenny, R.J.2    Krishnaswamy, S.3
  • 3
    • 0023858573 scopus 로고
    • Prothrombinase complex assembly. Kinetic mechanism of enzyme assembly on phospholipid vesicles
    • Krishnaswamy, S., Jones, K. C., and Mann, K. G. (1988) Prothrombinase complex assembly. Kinetic mechanism of enzyme assembly on phospholipid vesicles. J. Biol. Chem. 263, 3823-3834
    • (1988) J. Biol. Chem. , vol.263 , pp. 3823-3834
    • Krishnaswamy, S.1    Jones, K.C.2    Mann, K.G.3
  • 4
    • 0025217011 scopus 로고
    • Prothrombinase complex assembly. Contributions of protein-protein and protein-membrane interactions toward complex formation
    • Krishnaswamy, S. (1990) Prothrombinase complex assembly. Contributions of protein-protein and protein-membrane interactions toward complex formation. J. Biol. Chem. 265, 3708-3718
    • (1990) J. Biol. Chem. , vol.265 , pp. 3708-3718
    • Krishnaswamy, S.1
  • 5
    • 0015787418 scopus 로고
    • A polypeptide region of bovine prothrombin specific for binding to phospholipids
    • Gitel, S. N., Owen, W. G., Esmon, C. T., and Jackson, C. M. (1973) A polypeptide region of bovine prothrombin specific for binding to phospholipids. Proc. Natl. Acad. Sci. U.S.A. 70, 1344-1348
    • (1973) Proc. Natl. Acad. Sci. U.S.A. , vol.70 , pp. 1344-1348
    • Gitel, S.N.1    Owen, W.G.2    Esmon, C.T.3    Jackson, C.M.4
  • 7
    • 0031043059 scopus 로고    scopus 로고
    • Pathophysiologic implications of membrane phospholipid asymmetry in blood cells
    • Zwaal, R. F., and Schroit, A. J. (1997) Pathophysiologic implications of membrane phospholipid asymmetry in blood cells. Blood 89, 1121-1132
    • (1997) Blood , vol.89 , pp. 1121-1132
    • Zwaal, R.F.1    Schroit, A.J.2
  • 8
    • 84884790640 scopus 로고    scopus 로고
    • Rare inherited coagulation disorders other than hemophilia
    • (Marder, V. J., Aird, W. C., Bennett, J. S., and White, G. C., eds) , Lippincott Williams & Wilkins, Philadelphia
    • Mannucci, P. M., Peyvandi, F., and Franchini, M. (2013) Rare inherited coagulation disorders other than hemophilia. in Hemostasis and Thrombosis: Basic Principles and Clinical Practice (Marder, V. J., Aird, W. C., Bennett, J. S., and White, G. C., eds) pp. 685-692, Lippincott Williams & Wilkins, Philadelphia
    • (2013) Hemostasis and Thrombosis: Basic Principles and Clinical Practice , pp. 685-692
    • Mannucci, P.M.1    Peyvandi, F.2    Franchini, M.3
  • 9
    • 84884776617 scopus 로고    scopus 로고
    • Vitamin K antagonists. Biochemistry, pharmacology, and management
    • (Marder, V. J., Aird, W. C., Bennett, J. S., and White, G. C., eds) Lippincott Williams&Wilkins, Philadelphia
    • Shah, N., Ortel, T. L., and Schulman, S. (2013) Vitamin K antagonists. Biochemistry, pharmacology, and management. in Hemostasis and Thrombosis: Basic Principles and Clinical Practice (Marder, V. J., Aird, W. C., Bennett, J. S., and White, G. C., eds) Lippincott Williams&Wilkins, pp. 1267-1280, Philadelphia
    • (2013) Hemostasis and Thrombosis: Basic Principles and Clinical Practice , pp. 1267-1280
    • Shah, N.1    Ortel, T.L.2    Schulman, S.3
  • 10
    • 0021278877 scopus 로고
    • "Clotspeed," a mathematical simulation of the functional properties of prothrombinase
    • Nesheim, M. E., Tracy, R. P., and Mann, K. G. (1984) "Clotspeed, " a mathematical simulation of the functional properties of prothrombinase. J. Biol. Chem. 259, 1447-1453
    • (1984) J. Biol. Chem. , vol.259 , pp. 1447-1453
    • Nesheim, M.E.1    Tracy, R.P.2    Mann, K.G.3
  • 12
    • 0028032579 scopus 로고
    • The activation of prothrombin by the prothrombinase complex. The contribution of the substrate-membrane interaction to catalysis
    • Walker, R. K., and Krishnaswamy, S. (1994) The activation of prothrombin by the prothrombinase complex. The contribution of the substrate-membrane interaction to catalysis. J. Biol. Chem. 269, 27441-27450
    • (1994) J. Biol. Chem. , vol.269 , pp. 27441-27450
    • Walker, R.K.1    Krishnaswamy, S.2
  • 13
    • 0025314261 scopus 로고
    • Studies of the role of factor Va in the factor Xa-catalyzed activation of prothrombin, fragment 1.2-prethrombin-2, and dansyl-L-glutamyl-glycyl-L- argininemeizothrombin in the absence of phospholipids
    • Boskovic, D. S., Giles, A. R., and Nesheim, M. E. (1990) Studies of the role of factor Va in the factor Xa-catalyzed activation of prothrombin, fragment 1.2-prethrombin-2, and dansyl-L-glutamyl-glycyl-L-argininemeizothrombin in the absence of phospholipid. J. Biol. Chem. 265, 10497-10505
    • (1990) J. Biol. Chem. , vol.265 , pp. 10497-10505
    • Boskovic, D.S.1    Giles, A.R.2    Nesheim, M.E.3
  • 14
    • 84880586902 scopus 로고    scopus 로고
    • The transition of prothrombin to thrombin
    • Krishnaswamy, S. (2013) The transition of prothrombin to thrombin. J. Thromb. Haemost. 11, 265-276
    • (2013) J. Thromb. Haemost. , vol.11 , pp. 265-276
    • Krishnaswamy, S.1
  • 15
    • 11144229671 scopus 로고    scopus 로고
    • Binding of substrate in two conformations to human prothrombinase drives consecutive cleavage at two sites in prothrombin
    • Orcutt, S. J., and Krishnaswamy, S. (2004) Binding of substrate in two conformations to human prothrombinase drives consecutive cleavage at two sites in prothrombin. J. Biol. Chem. 279, 54927-54936
    • (2004) J. Biol. Chem. , vol.279 , pp. 54927-54936
    • Orcutt, S.J.1    Krishnaswamy, S.2
  • 16
    • 73649097569 scopus 로고    scopus 로고
    • Regulated cleavage of prothrombin by prothrombinase. Repositioning a cleavage site reveals the unique kinetic behavior of the action of prothrombinase on its compound substrate
    • Bradford, H. N., Micucci, J. A., and Krishnaswamy, S. (2010) Regulated cleavage of prothrombin by prothrombinase. Repositioning a cleavage site reveals the unique kinetic behavior of the action of prothrombinase on its compound substrate. J. Biol. Chem. 285, 328-338
    • (2010) J. Biol. Chem. , vol.285 , pp. 328-338
    • Bradford, H.N.1    Micucci, J.A.2    Krishnaswamy, S.3
  • 17
    • 22544469092 scopus 로고    scopus 로고
    • Ratcheting of the substrate from the zymogen to proteinase conformations directs the sequential cleavage of prothrombin by prothrombinase
    • Bianchini, E. P., Orcutt, S. J., Panizzi, P., Bock, P. E., and Krishnaswamy, S. (2005) Ratcheting of the substrate from the zymogen to proteinase conformations directs the sequential cleavage of prothrombin by prothrombinase. Proc. Natl. Acad. Sci. U.S.A. 102, 10099-10104
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 10099-10104
    • Bianchini, E.P.1    Orcutt, S.J.2    Panizzi, P.3    Bock, P.E.4    Krishnaswamy, S.5
  • 18
    • 17644371341 scopus 로고    scopus 로고
    • Exosite-driven substrate specificity and function in coagulation
    • Krishnaswamy, S. (2005) Exosite-driven substrate specificity and function in coagulation. J. Thromb. Haemost. 3, 54-67
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 54-67
    • Krishnaswamy, S.1
  • 19
    • 34250778996 scopus 로고    scopus 로고
    • Exosites in the substrate specificity of blood coagulation reactions
    • Bock, P. E., Panizzi, P., and Verhamme, I. M. (2007) Exosites in the substrate specificity of blood coagulation reactions. J. Thromb. Haemost. 5, 81-94
    • (2007) J. Thromb. Haemost. , vol.5 , pp. 81-94
    • Bock, P.E.1    Panizzi, P.2    Verhamme, I.M.3
  • 20
    • 0021915109 scopus 로고
    • The kinetics of activation of normal and β-carboxyglutamic acid-deficient prothrombins
    • Malhotra, O. P., Nesheim, M. E., and Mann, K. G. (1985) The kinetics of activation of normal and β-carboxyglutamic acid-deficient prothrombins. J. Biol. Chem. 260, 279-287
    • (1985) J. Biol. Chem. , vol.260 , pp. 279-287
    • Malhotra, O.P.1    Nesheim, M.E.2    Mann, K.G.3
  • 21
    • 0027522301 scopus 로고
    • Thioester peptide chloromethyl ketones. Reagents for active site-selective labeling of serine proteases with spectroscopic probes
    • Bock, P. E. (1993) Thioester peptide chloromethyl ketones. Reagents for active site-selective labeling of serine proteases with spectroscopic probes. Methods Enzymol. 222, 478-503
    • (1993) Methods Enzymol. , vol.222 , pp. 478-503
    • Bock, P.E.1
  • 22
    • 0001022995 scopus 로고
    • A modification of the colorimetric phosphorus determination for use with the photoelectric colorimeter
    • Gomori, G. (1942) A modification of the colorimetric phosphorus determination for use with the photoelectric colorimeter. J. Lab. Clin. Med. 27, 955-960
    • (1942) J. Lab. Clin. Med. , vol.27 , pp. 955-960
    • Gomori, G.1
  • 23
    • 0030057434 scopus 로고    scopus 로고
    • Role of the activation peptide domain in human factor X activation by the extrinsic Xase complex
    • Baugh, R. J., and Krishnaswamy, S. (1996) Role of the activation peptide domain in human factor X activation by the extrinsic Xase complex. J. Biol. Chem. 271, 16126-16134
    • (1996) J. Biol. Chem. , vol.271 , pp. 16126-16134
    • Baugh, R.J.1    Krishnaswamy, S.2
  • 24
    • 2242455930 scopus 로고    scopus 로고
    • Extended interactions with prothrombinase enforce affinity and specificity for its macromolecular substrate
    • Orcutt, S. J., Pietropaolo, C., and Krishnaswamy, S. (2002) Extended interactions with prothrombinase enforce affinity and specificity for its macromolecular substrate. J. Biol. Chem. 277, 46191-46196
    • (2002) J. Biol. Chem. , vol.277 , pp. 46191-46196
    • Orcutt, S.J.1    Pietropaolo, C.2    Krishnaswamy, S.3
  • 25
    • 0037135531 scopus 로고    scopus 로고
    • Nematode anticoagulant protein c2 reveals a site on factor Xa that is important for macromolecular substrate binding to human prothrombinase
    • Buddai, S. K., Toulokhonova, L., Bergum, P. W., Vlasuk, G. P., and Krishnaswamy, S. (2002) Nematode anticoagulant protein c2 reveals a site on factor Xa that is important for macromolecular substrate binding to human prothrombinase. J. Biol. Chem. 277, 26689-26698
    • (2002) J. Biol. Chem. , vol.277 , pp. 26689-26698
    • Buddai, S.K.1    Toulokhonova, L.2    Bergum, P.W.3    Vlasuk, G.P.4    Krishnaswamy, S.5
  • 27
    • 0028287885 scopus 로고
    • Assembly of the prothrombinase complex enhances the inhibition of bovine factor Xa by tick anticoagulant peptide
    • Krishnaswamy, S., Vlasuk, G. P., and Bergum, P. W. (1994) Assembly of the prothrombinase complex enhances the inhibition of bovine factor Xa by tick anticoagulant peptide. Biochemistry 33, 7897-7907
    • (1994) Biochemistry , vol.33 , pp. 7897-7907
    • Krishnaswamy, S.1    Vlasuk, G.P.2    Bergum, P.W.3
  • 28
    • 0020651713 scopus 로고
    • Analysis for β-carboxyglutamic acid
    • Price, P. A. (1983) Analysis for β-carboxyglutamic acid. Methods Enzymol. 91, 13-17
    • (1983) Methods Enzymol. , vol.91 , pp. 13-17
    • Price, P.A.1
  • 29
    • 0034623944 scopus 로고    scopus 로고
    • Exosite binding tethers the macromolecular substrate to the prothrombinase complex and directs cleavage at two spatially distinct sites
    • Boskovic, D. S., and Krishnaswamy, S. (2000) Exosite binding tethers the macromolecular substrate to the prothrombinase complex and directs cleavage at two spatially distinct sites. J. Biol. Chem. 275, 38561-38570
    • (2000) J. Biol. Chem. , vol.275 , pp. 38561-38570
    • Boskovic, D.S.1    Krishnaswamy, S.2
  • 31
    • 0017762527 scopus 로고
    • Activation of human factor X (Stuart factor) by a protease from Russell's viper venom
    • Di Scipio, R. G., Hermodson, M. A., and Davie, E. W. (1977) Activation of human factor X (Stuart factor) by a protease from Russell's viper venom. Biochemistry 16, 5253-5260
    • (1977) Biochemistry , vol.16 , pp. 5253-5260
    • Di Scipio, R.G.1    Hermodson, M.A.2    Davie, E.W.3
  • 33
    • 2442655492 scopus 로고    scopus 로고
    • Removal of B-domain sequences from factor v rather than specific proteolysis underlies the mechanism by which cofactor function is realized
    • Toso, R., and Camire, R. M. (2004) Removal of B-domain sequences from factor V rather than specific proteolysis underlies the mechanism by which cofactor function is realized. J. Biol. Chem. 279, 21643-21650
    • (2004) J. Biol. Chem. , vol.279 , pp. 21643-21650
    • Toso, R.1    Camire, R.M.2
  • 34
    • 84865763235 scopus 로고    scopus 로고
    • Meizothrombin is an unexpectedly zymogen-like variant of thrombin
    • Bradford, H. N., and Krishnaswamy, S. (2012) Meizothrombin is an unexpectedly zymogen-like variant of thrombin. J. Biol. Chem. 287, 30414-30425
    • (2012) J. Biol. Chem. , vol.287 , pp. 30414-30425
    • Bradford, H.N.1    Krishnaswamy, S.2
  • 35
    • 0030767267 scopus 로고    scopus 로고
    • Exosites determine macromolecular substrate recognition by prothrombinase
    • Krishnaswamy, S., and Betz, A. (1997) Exosites determine macromolecular substrate recognition by prothrombinase. Biochemistry 36, 12080-12086
    • (1997) Biochemistry , vol.36 , pp. 12080-12086
    • Krishnaswamy, S.1    Betz, A.2
  • 36
    • 0037402223 scopus 로고    scopus 로고
    • A logarithmic approximation to initial rates of enzyme reactions
    • Lu, W. P., and Fei, L. (2003) A logarithmic approximation to initial rates of enzyme reactions. Anal. Biochem. 316, 58-65
    • (2003) Anal. Biochem. , vol.316 , pp. 58-65
    • Lu, W.P.1    Fei, L.2
  • 37
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data. Application to HIV proteinase
    • Kuzmic, P. (1996) Program DYNAFIT for the analysis of enzyme kinetic data. Application to HIV proteinase. Anal. Biochem. 237, 260-273
    • (1996) Anal. Biochem. , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 39
    • 36349026346 scopus 로고    scopus 로고
    • Restricted active site docking by enzyme-bound substrate enforces the ordered cleavage of prothrombin by prothrombinase
    • Hacisalihoglu, A., Panizzi, P., Bock, P. E., Camire, R. M., and Krishnaswamy, S. (2007) Restricted active site docking by enzyme-bound substrate enforces the ordered cleavage of prothrombin by prothrombinase. J. Biol. Chem. 282, 32974-32982
    • (2007) J. Biol. Chem. , vol.282 , pp. 32974-32982
    • Hacisalihoglu, A.1    Panizzi, P.2    Bock, P.E.3    Camire, R.M.4    Krishnaswamy, S.5
  • 40
    • 79551628274 scopus 로고    scopus 로고
    • Prothrombin activation on the activated platelet surface optimizes expression of procoagulant activity
    • Wood, J. P., Silveira, J. R., Maille, N. M., Haynes, L. M., and Tracy, P. B. (2011) Prothrombin activation on the activated platelet surface optimizes expression of procoagulant activity. Blood 117, 1710-1718
    • (2011) Blood , vol.117 , pp. 1710-1718
    • Wood, J.P.1    Silveira, J.R.2    Maille, N.M.3    Haynes, L.M.4    Tracy, P.B.5
  • 41
    • 0034528766 scopus 로고    scopus 로고
    • The Gla domain of human prothrombin has a binding site for factor Va
    • Blostein, M. D., Rigby, A. C., Jacobs, M., Furie, B., and Furie, B. C. (2000) The Gla domain of human prothrombin has a binding site for factor Va. J. Biol. Chem. 275, 38120-38126
    • (2000) J. Biol. Chem. , vol.275 , pp. 38120-38126
    • Blostein, M.D.1    Rigby, A.C.2    Jacobs, M.3    Furie, B.4    Furie, B.C.5
  • 42
    • 84869015264 scopus 로고    scopus 로고
    • Prothrombin activation by platelet-associated prothrombinase proceeds through the prethrombin-2 pathway via a concerted mechanism
    • Haynes, L. M., Bouchard, B. A., Tracy, P. B., and Mann, K. G. (2012) Prothrombin activation by platelet-associated prothrombinase proceeds through the prethrombin-2 pathway via a concerted mechanism. J. Biol. Chem. 287, 38647-38655
    • (2012) J. Biol. Chem. , vol.287 , pp. 38647-38655
    • Haynes, L.M.1    Bouchard, B.A.2    Tracy, P.B.3    Mann, K.G.4
  • 43
    • 0037470249 scopus 로고    scopus 로고
    • Analysis of the kinetics of prothrombin activation and evidence that two equilibrating forms of prothrombinase are involved in the process
    • Brufatto, N., and Nesheim, M. E. (2003) Analysis of the kinetics of prothrombin activation and evidence that two equilibrating forms of prothrombinase are involved in the process. J. Biol. Chem. 278, 6755-6764
    • (2003) J. Biol. Chem. , vol.278 , pp. 6755-6764
    • Brufatto, N.1    Nesheim, M.E.2
  • 44
    • 36349000220 scopus 로고    scopus 로고
    • Further evidence for two functional forms of prothrombinase each specific for either of the two prothrombin activation cleavages
    • Kim, P. Y., and Nesheim, M. E. (2007) Further evidence for two functional forms of prothrombinase each specific for either of the two prothrombin activation cleavages. J. Biol. Chem. 282, 32568-32581
    • (2007) J. Biol. Chem. , vol.282 , pp. 32568-32581
    • Kim, P.Y.1    Nesheim, M.E.2
  • 45
    • 77952674090 scopus 로고    scopus 로고
    • A revisit to the one form kinetic model of prothrombinase
    • Lee, C. J., Wu, S., Eun, C., and Pedersen, L. G. (2010) A revisit to the one form kinetic model of prothrombinase. Biophys. Chem. 149, 28-33
    • (2010) Biophys. Chem. , vol.149 , pp. 28-33
    • Lee, C.J.1    Wu, S.2    Eun, C.3    Pedersen, L.G.4
  • 46
    • 0025840544 scopus 로고
    • Meizothrombin formation during factor Xa-catalyzed prothrombin activation. Formation in a purified system and in plasma
    • Tans, G., Janssen-Claessen, T., Hemker, H. C., Zwaal, R. F., and Rosing, J. (1991) Meizothrombin formation during factor Xa-catalyzed prothrombin activation. Formation in a purified system and in plasma. J. Biol. Chem. 266, 21864-21873
    • (1991) J. Biol. Chem. , vol.266 , pp. 21864-21873
    • Tans, G.1    Janssen-Claessen, T.2    Hemker, H.C.3    Zwaal, R.F.4    Rosing, J.5
  • 47
    • 0025844953 scopus 로고
    • Formation of meizothrombin as intermediate in factor Xa-catalyzed prothrombin activation on endothelial cells. The influence of thrombin on the reaction mechanism
    • Tijburg, P. N., van Heerde, W. L., Leenhouts, H. M., Hessing, M., Bouma, B. N., and de Groot, P. G. (1991) Formation of meizothrombin as intermediate in factor Xa-catalyzed prothrombin activation on endothelial cells. The influence of thrombin on the reaction mechanism. J. Biol. Chem. 266, 4017-4022
    • (1991) J. Biol. Chem. , vol.266 , pp. 4017-4022
    • Tijburg, P.N.1    Van Heerde, W.L.2    Leenhouts, H.M.3    Hessing, M.4    Bouma, B.N.5    De Groot, P.G.6
  • 48
    • 0029803229 scopus 로고    scopus 로고
    • Protein C activation on endothelial cells by prothrombin activation products generated in situ. Meizothrombin is a better protein C activator than β-thrombin
    • Hackeng, T. M., Tans, G., Koppelman, S. J., de Groot, P. G., Rosing, J., and Bouma, B. N. (1996) Protein C activation on endothelial cells by prothrombin activation products generated in situ. Meizothrombin is a better protein C activator than β-thrombin. Biochem. J. 319, 399-405
    • (1996) Biochem. J. , vol.319 , pp. 399-405
    • Hackeng, T.M.1    Tans, G.2    Koppelman, S.J.3    De Groot, P.G.4    Rosing, J.5    Bouma, B.N.6
  • 49
    • 0017663278 scopus 로고
    • A spectrum of partially carboxylated prothrombins in the plasmas of coumarin-treated patients
    • Friedman, P. A., Rosenberg, R. D., Hauschka, P. V., and Fitz-James, A. (1977) A spectrum of partially carboxylated prothrombins in the plasmas of coumarin-treated patients. Biochim. Biophys. Acta 494, 271-276
    • (1977) Biochim. Biophys. Acta , vol.494 , pp. 271-276
    • Friedman, P.A.1    Rosenberg, R.D.2    Hauschka, P.V.3    Fitz-James, A.4
  • 50
    • 84881227791 scopus 로고    scopus 로고
    • Crystal Structure of prothrombin reveals conformational flexibility and mechanism of activation
    • Pozzi, N., Chen, Z., Gohara, D. W., Niu, W., Heyduk, T., and Di Cera, E. (2013) Crystal Structure of prothrombin reveals conformational flexibility and mechanism of activation. J. Biol. Chem. 288, 22734-22744
    • (2013) J. Biol. Chem. , vol.288 , pp. 22734-22744
    • Pozzi, N.1    Chen, Z.2    Gohara, D.W.3    Niu, W.4    Heyduk, T.5    Di Cera, E.6
  • 51
    • 0023196008 scopus 로고
    • Activation of human prothrombin by human prothrombinase. Influence of factor Va on the reaction mechanism
    • Krishnaswamy, S., Church, W. R., Nesheim, M. E., and Mann, K. G. (1987) Activation of human prothrombin by human prothrombinase. Influence of factor Va on the reaction mechanism. J. Biol. Chem. 262, 3291-3299
    • (1987) J. Biol. Chem. , vol.262 , pp. 3291-3299
    • Krishnaswamy, S.1    Church, W.R.2    Nesheim, M.E.3    Mann, K.G.4
  • 52
    • 0024263049 scopus 로고
    • Meizothrombin, a major product of factor Xa-catalyzed prothrombin activation
    • Rosing, J., and Tans, G. (1988) Meizothrombin, a major product of factor Xa-catalyzed prothrombin activation. Thromb. Haemost. 60, 355-360
    • (1988) Thromb. Haemost. , vol.60 , pp. 355-360
    • Rosing, J.1    Tans, G.2
  • 54
    • 0027435759 scopus 로고
    • Meizothrombin. Active intermediate formed during prothrombinase-catalyzed activation of prothrombin
    • Doyle, M. F., and Haley, P. E. (1993) Meizothrombin. Active intermediate formed during prothrombinase-catalyzed activation of prothrombin. Methods Enzymol. 222, 299-312
    • (1993) Methods Enzymol. , vol.222 , pp. 299-312
    • Doyle, M.F.1    Haley, P.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.