메뉴 건너뛰기




Volumn 287, Issue 8, 2012, Pages 5225-5234

Membrane binding events in the initiation and propagation phases of tissue factor-initiated zymogen activation under flow

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE REGIONS; COAGULATION PROCESS; ENZYME MEMBRANES; FACTOR X; FACTOR XA; FLOW CONDITION; INITIATION AND PROPAGATION; LIMITING FACTORS; MEMBRANE BINDING; MEMBRANE BINDING EVENTS; PROTHROMBINASE; RATE LIMITING; STEADY-STATE MODELS; VASCULATURE; ZYMOGEN ACTIVATION;

EID: 84857302217     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.302075     Document Type: Article
Times cited : (19)

References (58)
  • 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 (Pubitemid 20220784)
    • (1990) Blood , vol.76 , Issue.1 , pp. 1-16
    • Mann, K.G.1    Nesheim, M.E.2    Church, K.R.3    Haley, P.4    Krishnaswamy, S.5
  • 2
    • 0027104537 scopus 로고
    • The interaction of human factor VIIa with tissue factor
    • Krishnaswamy, S. (1992) The interaction of human factor VIIa with tissue factor. J. Biol. Chem. 267, 23696-23706
    • (1992) J. Biol. Chem. , vol.267 , pp. 23696-23706
    • Krishnaswamy, S.1
  • 3
    • 0017660808 scopus 로고
    • Kinetics of the activation of bovine coagulation factor X by components of the extrinsic pathway. Kinetic behavior of two chain factor VII in the presence and absence of tissue factor
    • Silverberg, S. A., Nemerson, Y., and Zur, M. (1977) Kinetics of the activation of bovine coagulation factor X by components of the extrinsic pathway. Kinetic behavior of two-chain factor VII in the presence and absence of tissue factor. J. Biol. Chem. 252, 8481-8488 (Pubitemid 8243725)
    • (1977) Journal of Biological Chemistry , vol.252 , Issue.23 , pp. 8481-8488
    • Silverberg, S.A.1    Nemerson, Y.2    Zur, M.3
  • 5
    • 0037231876 scopus 로고    scopus 로고
    • Influence of factor VIIa and phospholipids on coagulation in "acquired" hemophilia
    • DOI 10.1161/01.ATV.0000042081.57854.A2
    • Butenas, S., Brummel, K. E., Paradis, S. G., and Mann, K. G. (2003) Influence of factor VIIa and phospholipids on coagulation in "acquired" hemophilia. Arterioscler. Thromb. Vasc. Biol. 23, 123-129 (Pubitemid 36091636)
    • (2003) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.23 , Issue.1 , pp. 123-129
    • Butenas, S.1    Brummel, K.E.2    Paradis, S.G.3    Mann, K.G.4
  • 6
    • 0018622772 scopus 로고
    • The contribution of bovine factor V and factor Va to the activity of prothrombinase
    • Nesheim, M. E., Taswell, J. B., and Mann, K. G. (1979) The contribution of bovine factor V and factor Va to the activity of prothrombinase. J. Biol. Chem. 254, 10952-10962 (Pubitemid 10163282)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.21 , pp. 10952-10962
    • Nesheim, M.E.1    Taswell, J.B.2    Mann, K.G.3
  • 7
    • 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 (Pubitemid 14104191)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.3 , pp. 1447-1453
    • Nesheim, M.E.1    Tracy, R.P.2    Mann, K.G.3
  • 8
    • 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 (Pubitemid 18078974)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.8 , pp. 3823-3834
    • Krishnaswamy, S.1    Jones, K.C.2    Mann, K.G.3
  • 9
    • 0018814280 scopus 로고
    • The kinetics of immobilized enzyme systems
    • Laidler, K. J., and Bunting, P. S. (1980) The kinetics of immobilized enzyme systems. Methods Enzymol. 64, 227-248
    • (1980) Methods Enzymol. , vol.64 , pp. 227-248
    • Laidler, K.J.1    Bunting, P.S.2
  • 10
    • 0015978781 scopus 로고
    • Theory of the kinetics of reactions catalyzed by enzymes attached to the interior surfaces of tubes
    • Koyayashi, T., and Laidler, K. J. (1974) Theory of the kinetics of reactions catalyzed by enzymes attached to the interior surfaces of tubes. Biotechnol. Bioeng. 16, 99-118
    • (1974) Biotechnol. Bioeng. , vol.16 , pp. 99-118
    • Koyayashi, T.1    Laidler, K.J.2
  • 11
    • 0015956518 scopus 로고
    • Theory of the kinetics of reactions catalyzed by enzymes attached to membranes
    • Kobayashi, T., and Laidler, K. J. (1974) Theory of the kinetics of reactions catalyzed by enzymes attached to membranes. Biotechnol. Bioeng. 16, 77-97
    • (1974) Biotechnol. Bioeng. , vol.16 , pp. 77-97
    • Kobayashi, T.1    Laidler, K.J.2
  • 12
    • 0015951362 scopus 로고
    • Flow kinetics of L-asparaginase attached to nylon tubing
    • Bunting, P. S., and Laidler, K. J. (1974) Flow kinetics of L-asparaginase attached to nylon tubing. Biotechnol. Bioeng. 16, 119-134
    • (1974) Biotechnol. Bioeng. , vol.16 , pp. 119-134
    • Bunting, P.S.1    Laidler, K.J.2
  • 13
    • 33746854743 scopus 로고    scopus 로고
    • Flow effects on coagulation and thrombosis
    • Hathcock, J. J. (2006) Flow effects on coagulation and thrombosis. Arterioscler. Thromb. Vasc. Biol. 26, 1729-1737
    • (2006) Arterioscler. Thromb. Vasc. Biol. , vol.26 , pp. 1729-1737
    • Hathcock, J.J.1
  • 14
    • 77949274557 scopus 로고    scopus 로고
    • Tissue factor activity under flow
    • Diamond, S. L. (2010) Tissue factor activity under flow. Thromb. Res. 125, Suppl. 1, S29-S30
    • (2010) Thromb. Res. , vol.125 , Issue.SUPPL. 1
    • Diamond, S.L.1
  • 15
    • 43549100702 scopus 로고    scopus 로고
    • Determination of surface tissue factor thresholds that trigger coagulation at venous and arterial shear rates. Amplification of 100 fM circulating tissue factor requires flow
    • Okorie, U. M., Denney, W. S., Chatterjee, M. S., Neeves, K. B., and Diamond, S. L. (2008) Determination of surface tissue factor thresholds that trigger coagulation at venous and arterial shear rates. Amplification of 100 fM circulating tissue factor requires flow. Blood 111, 3507-3513
    • (2008) Blood , vol.111 , pp. 3507-3513
    • Okorie, U.M.1    Denney, W.S.2    Chatterjee, M.S.3    Neeves, K.B.4    Diamond, S.L.5
  • 16
    • 35348953113 scopus 로고    scopus 로고
    • Characterization of the threshold response of initiation of blood clotting to stimulus patch size
    • DOI 10.1529/biophysj.107.109009
    • Kastrup, C. J., Shen, F., Runyon, M. K., and Ismagilov, R. F. (2007) Characterization of the threshold response of initiation of blood clotting to stimulus patch size. Biophys. J. 93, 2969-2977 (Pubitemid 47607831)
    • (2007) Biophysical Journal , vol.93 , Issue.8 , pp. 2969-2977
    • Kastrup, C.J.1    Shen, F.2    Runyon, M.K.3    Ismagilov, R.F.4
  • 17
    • 55449124272 scopus 로고    scopus 로고
    • Threshold response of initiation of blood coagulation by tissue factor in patterned microfluidic capillaries is controlled by shear rate
    • Shen, F., Kastrup, C. J., Liu, Y., and Ismagilov, R. F. (2008) Threshold response of initiation of blood coagulation by tissue factor in patterned microfluidic capillaries is controlled by shear rate. Arterioscler. Thromb. Vasc. Biol. 28, 2035-2041
    • (2008) Arterioscler. Thromb. Vasc. Biol. , vol.28 , pp. 2035-2041
    • Shen, F.1    Kastrup, C.J.2    Liu, Y.3    Ismagilov, R.F.4
  • 18
    • 41449101562 scopus 로고    scopus 로고
    • Effects of shear rate on propagation of blood clotting determined using microfluidics and numerical simulations
    • DOI 10.1021/ja076301r
    • Runyon, M. K., Kastrup, C. J., Johnson-Kerner, B. L., Ha, T. G., and Ismagilov, R. F. (2008) Effects of shear rate on propagation of blood clotting determined using microfluidics and numerical simulations. J. Am. Chem. Soc. 130, 3458-3464 (Pubitemid 351456047)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.11 , pp. 3458-3464
    • Runyon, M.K.1    Kastrup, C.J.2    Johnson-Kerner, B.L.3    Van Ha, T.G.4    Ismagilov, R.F.5
  • 19
    • 80052495060 scopus 로고    scopus 로고
    • Simulated surface-induced thrombin generation in a flow field
    • Jordan, S. W., and Chaikof, E. L. (2011) Simulated surface-induced thrombin generation in a flow field. Biophys. J. 101, 276-286
    • (2011) Biophys. J. , vol.101 , pp. 276-286
    • Jordan, S.W.1    Chaikof, E.L.2
  • 20
    • 79952603824 scopus 로고    scopus 로고
    • Grow with the flow. A spatialtemporal model of platelet deposition and blood coagulation under flow
    • Leiderman, K., and Fogelson, A. L. (2011) Grow with the flow. A spatialtemporal model of platelet deposition and blood coagulation under flow. Math. Med. Biol. 28, 47-84
    • (2011) Math. Med. Biol. , vol.28 , pp. 47-84
    • Leiderman, K.1    Fogelson, A.L.2
  • 21
    • 31344462420 scopus 로고    scopus 로고
    • Coagulation under flow. The influence of flow-mediated transport on the initiation and inhibition of coagulation
    • Fogelson, A. L., and Tania, N. (2005) Coagulation under flow. The influence of flow-mediated transport on the initiation and inhibition of coagulation. Pathophysiol. Haemost. Thromb. 34, 91-108
    • (2005) Pathophysiol. Haemost. Thromb. , vol.34 , pp. 91-108
    • Fogelson, A.L.1    Tania, N.2
  • 22
    • 0035119193 scopus 로고    scopus 로고
    • Surface-mediated control of blood coagulation: The role of binding site densities and platelet deposition
    • Kuharsky, A. L., and Fogelson, A. L. (2001) Surface-mediated control of blood coagulation. The role of binding site densities and platelet deposition. Biophys. J. 80, 1050-1074 (Pubitemid 32182136)
    • (2001) Biophysical Journal , vol.80 , Issue.3 , pp. 1050-1074
    • Kuharsky, A.L.1    Fogelson, A.L.2
  • 23
    • 79551659654 scopus 로고    scopus 로고
    • Dilutional control of prothrombin activation at physiologically relevant shear rates
    • Haynes, L. M., Dubief, Y. C., Orfeo, T., and Mann, K. G. (2011) Dilutional control of prothrombin activation at physiologically relevant shear rates. Biophys. J. 100, 765-773
    • (2011) Biophys. J. , vol.100 , pp. 765-773
    • Haynes, L.M.1    Dubief, Y.C.2    Orfeo, T.3    Mann, K.G.4
  • 24
    • 0025652030 scopus 로고
    • Continuous flow and the prothrombinase-catalyzed activation of prothrombin
    • Schoen, P., Lindhout, T., Willems, G., and Hemker, H. C. (1990) Continuous flow and the prothrombinase-catalyzed activation of prothrombin. Thromb. Haemost. 64, 542-547
    • (1990) Thromb. Haemost. , vol.64 , pp. 542-547
    • Schoen, P.1    Lindhout, T.2    Willems, G.3    Hemker, H.C.4
  • 25
    • 0028821466 scopus 로고
    • Prothrombin activation by prothrombinase in a tubular flow reactor
    • Billy, D., Speijer, H., Willems, G., Hemker, H. C., and Lindhout, T. (1995) Prothrombin activation by prothrombinase in a tubular flow reactor. J. Biol. Chem. 270, 1029-1034
    • (1995) J. Biol. Chem. , vol.270 , pp. 1029-1034
    • Billy, D.1    Speijer, H.2    Willems, G.3    Hemker, H.C.4    Lindhout, T.5
  • 26
    • 0025900914 scopus 로고
    • Flow and the inhibition of prothrombinase by antithrombin III and heparin
    • Schoen, P., and Lindhout, T. (1991) Flow and the inhibition of prothrombinase by antithrombin III and heparin. Blood 78, 118-124
    • (1991) Blood , vol.78 , pp. 118-124
    • Schoen, P.1    Lindhout, T.2
  • 29
    • 2942531447 scopus 로고    scopus 로고
    • The function of factor XI in tissue factor-initiated thrombin generation
    • Butenas, S., Dee, J. D., and Mann, K. G. (2003) The function of factor XI in tissue factor-initiated thrombin generation. J. Thromb. Haemost. 1, 2103-2111
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 2103-2111
    • Butenas, S.1    Dee, J.D.2    Mann, K.G.3
  • 30
    • 20144381883 scopus 로고    scopus 로고
    • Phospholipid regulates the activation of factor X by tissue factor/factor VIIa (TF/VIIa) via substrate and product interactions
    • DOI 10.1021/bi050338b
    • Hathcock, J. J., Rusinova, E., Gentry, R. D., Andree, H., and Nemerson, Y. (2005) Phospholipid regulates the activation of factor X by tissue factor/ factor VIIa (TF/VIIa) via substrate and product interactions. Biochemistry 44, 8187-8197 (Pubitemid 40776680)
    • (2005) Biochemistry , vol.44 , Issue.22 , pp. 8187-8197
    • Hathcock, J.J.1    Rusinova, E.2    Gentry, R.D.3    Andree, H.4    Nemerson, Y.5
  • 31
    • 34249094172 scopus 로고    scopus 로고
    • Lipid-bound factor Xa regulates tissue factor activity
    • DOI 10.1021/bi700136a
    • Hathcock, J., Rusinova, E., Vaananen, H., and Nemerson, Y. (2007) Lipidbound factor Xa regulates tissue factor activity. Biochemistry 46, 6134-6140 (Pubitemid 46799172)
    • (2007) Biochemistry , vol.46 , Issue.20 , pp. 6134-6140
    • Hathcock, J.1    Rusinova, E.2    Vaananen, H.3    Nemerson, Y.4
  • 32
    • 0020633335 scopus 로고
    • The interaction of bovine factor V and factor V-derived peptides with phospholipid vesicles
    • Higgins, D. L., and Mann, K. G. (1983) The interaction of bovine factor V and factor V-derived peptides with phospholipid vesicles. J. Biol. Chem. 258, 6503-6508 (Pubitemid 13106824)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.10 , pp. 6503-6508
    • Higgins, D.L.1    Mann, K.G.2
  • 34
    • 0015739824 scopus 로고
    • Simultaneous purification of bovine prothrombin and factor X. Activation of prothrombin by trypsin-activated factor X
    • Bajaj, S. P., and Mann, K. G. (1973) Simultaneous purification of bovine prothrombin and factor X. Activation of prothrombin by trypsin-activated factor X. J. Biol. Chem. 248, 7729-7741
    • (1973) J. Biol. Chem. , vol.248 , pp. 7729-7741
    • Bajaj, S.P.1    Mann, K.G.2
  • 35
    • 0024991650 scopus 로고
    • Regulation of coagulation by a multivalent Kunitz-type inhibitor
    • DOI 10.1021/bi00485a001
    • Broze, G. J., Jr., Girard, T. J., and Novotny, W. F. (1990) Regulation of coagulation by a multivalent Kunitz-type inhibitor. Biochemistry 29, 7539-7546 (Pubitemid 20279168)
    • (1990) Biochemistry , vol.29 , Issue.33 , pp. 7539-7546
    • Broze Jr., G.J.1    Girard, T.J.2    Novotny, W.F.3
  • 37
    • 0026512750 scopus 로고
    • Formation of supported planar bilayers by fusion of vesicles to supported phospholipid monolayers
    • Kalb, E., Frey, S., and Tamm, L. K. (1992) Formation of supported planar bilayers by fusion of vesicles to supported phospholipid monolayers. Biochim. Biophys. Acta 1103, 307-316
    • (1992) Biochim. Biophys. Acta , vol.1103 , pp. 307-316
    • Kalb, E.1    Frey, S.2    Tamm, L.K.3
  • 38
    • 0021947327 scopus 로고
    • Supported phospholipid bilayers
    • Tamm, L. K., and McConnell, H. M. (1985) Supported phospholipid bilayers. Biophys. J. 47, 105-113
    • (1985) Biophys. J. , vol.47 , pp. 105-113
    • Tamm, L.K.1    McConnell, H.M.2
  • 39
    • 77449161190 scopus 로고    scopus 로고
    • Carbohydrates and activity of natural and recombinant tissue factor
    • Krudysz-Amblo, J., Jennings, M. E., 2nd, Mann, K. G., and Butenas, S. (2010) Carbohydrates and activity of natural and recombinant tissue factor. J. Biol. Chem. 285, 3371-3382
    • (2010) J. Biol. Chem. , vol.285 , pp. 3371-3382
    • Krudysz-Amblo, J.1    Jennings II, M.E.2    Mann, K.G.3    Butenas, S.4
  • 41
    • 0029927812 scopus 로고    scopus 로고
    • Intrinsic curvature in normal and inverted lipid structures and in membranes
    • Marsh, D. (1996) Intrinsic curvature in normal and inverted lipid structures and in membranes. Biophys. J. 70, 2248-2255
    • (1996) Biophys. J. , vol.70 , pp. 2248-2255
    • Marsh, D.1
  • 42
    • 34250365394 scopus 로고    scopus 로고
    • The local phospholipid environment modulates the activation of blood clotting
    • DOI 10.1074/jbc.M607973200
    • Shaw, A. W., Pureza, V. S., Sligar, S. G., and Morrissey, J. H. (2007) The local phospholipid environment modulates the activation of blood clotting. J. Biol. Chem. 282, 6556-6563 (Pubitemid 47100852)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.9 , pp. 6556-6563
    • Shaw, A.W.1    Pureza, V.S.2    Sligar, S.G.3    Morrissey, J.H.4
  • 43
    • 0028099267 scopus 로고
    • A membrane-mediated catalytic event in prothrombin activation
    • Kung, C., Hayes, E., and Mann, K. G. (1994) A membrane-mediated catalytic event in prothrombin activation. J. Biol. Chem. 269, 25838-25848 (Pubitemid 24336284)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.41 , pp. 25838-25848
    • Kung, C.1    Hayes, E.2    Mann, K.G.3
  • 44
    • 0019835197 scopus 로고
    • Assembly of the prothrombinase complex in the absence of prothrombin
    • Nesheim, M. E., Eid, S., and Mann, K. G. (1981) Assembly of the prothrombinase complex in the absence of prothrombin. J. Biol. Chem. 256, 9874-9882 (Pubitemid 12176187)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.19 , pp. 9874-9882
    • Nesheim, M.E.1    Eid, S.2    Mann, K.G.3
  • 46
    • 0018907213 scopus 로고
    • The role of phospholipids and factor Va in the prothrombinase complex
    • Rosing, J., Tans, G., Govers-Riemslag, J. W., Zwaal, R. F., and Hemker, H. C. (1980) The role of phospholipids and factor Va in the prothrombinase complex. J. Biol. Chem. 255, 274-283 (Pubitemid 10146055)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.1 , pp. 274-283
    • Rosing, J.1    Tans, G.2    Govers-Riemslag, J.W.P.3
  • 47
    • 0025600894 scopus 로고
    • The effects of shear rate on the enzymatic activity of the tissue factor-factor VIIa complex
    • Gemmell, C. H., Nemerson, Y., and Turitto, V. (1990) The effects of shear rate on the enzymatic activity of the tissue factor-factor VIIa complex. Microvasc. Res. 40, 327-340
    • (1990) Microvasc. Res. , vol.40 , pp. 327-340
    • Gemmell, C.H.1    Nemerson, Y.2    Turitto, V.3
  • 48
    • 0034705005 scopus 로고    scopus 로고
    • Functional analyses of two cellular binding domains of bovine lactadherin
    • DOI 10.1021/bi992221r
    • Andersen, M. H., Graversen, H., Fedosov, S. N., Petersen, T. E., and Rasmussen, J. T. (2000) Functional analyses of two cellular binding domains of bovine lactadherin. Biochemistry 39, 6200-6206 (Pubitemid 30327097)
    • (2000) Biochemistry , vol.39 , Issue.20 , pp. 6200-6206
    • Andersen, M.H.1    Graversen, H.2    Fedosov, S.N.3    Petersen, T.E.4    Rasmussen, J.T.5
  • 49
    • 0038107373 scopus 로고    scopus 로고
    • Lactadherin inhibits enzyme complexes of blood coagulation by competing for phospholipid-binding sites
    • DOI 10.1182/blood-2002-07-1951
    • Shi, J., and Gilbert, G. E. (2003) Lactadherin inhibits enzyme complexes of blood coagulation by competing for phospholipid-binding sites. Blood 101, 2628-2636 (Pubitemid 36857623)
    • (2003) Blood , vol.101 , Issue.7 , pp. 2628-2636
    • Shi, J.1    Gilbert, G.E.2
  • 50
    • 0036660207 scopus 로고    scopus 로고
    • Thrombin functions during tissue factor-induced blood coagulation
    • DOI 10.1182/blood.V100.1.148
    • Brummel, K. E., Paradis, S. G., Butenas, S., and Mann, K. G. (2002) Thrombin functions during tissue factor-induced blood coagulation. Blood 100, 148-152 (Pubitemid 35177440)
    • (2002) Blood , vol.100 , Issue.1 , pp. 148-152
    • Brummel, K.E.1    Paradis, S.G.2    Butenas, S.3    Mann, K.G.4
  • 51
    • 0023685665 scopus 로고
    • Flow as a regulator of the activation of factor X by tissue factor
    • Gemmell, C. H., Turitto, V. T., and Nemerson, Y. (1988) Flow as a regulator of the activation of factor X by tissue factor. Blood 72, 1404-1406 (Pubitemid 18265912)
    • (1988) Blood , vol.72 , Issue.4 , pp. 1404-1406
    • Gemmell, C.H.1    Turitto, V.T.2    Nemerson, Y.3
  • 52
    • 0026447620 scopus 로고
    • Diffusion control in blood coagulation. Activation of factor X by factors IXa/VIIIa assembled on human monocyte membranes
    • McGee, M. P., Li, L. C., and Xiong, H. (1992) Diffusion control in blood coagulation. Activation of factor X by factors IXa/VIIIa assembled on human monocyte membranes. J. Biol. Chem. 267, 24333-24339
    • (1992) J. Biol. Chem. , vol.267 , pp. 24333-24339
    • McGee, M.P.1    Li, L.C.2    Xiong, H.3
  • 54
    • 0018780186 scopus 로고
    • Phospholipidbinding properties of bovine factor V and factor Va
    • Bloom, J. W., Nesheim, M. E., and Mann, K. G. (1979) Phospholipidbinding properties of bovine factor V and factor Va. Biochemistry 18, 4419-4425
    • (1979) Biochemistry , vol.18 , pp. 4419-4425
    • Bloom, J.W.1    Nesheim, M.E.2    Mann, K.G.3
  • 55
    • 73649178367 scopus 로고
    • Preparation of human plasma prothrombin and some of its sedimentation properties
    • Lanchantin, G. F., Friedmann, J. A., DeGroot, J., and Mehl, J. W. (1963) Preparation of human plasma prothrombin and some of its sedimentation properties. J. Biol. Chem. 238, 238-243
    • (1963) J. Biol. Chem. , vol.238 , pp. 238-243
    • Lanchantin, G.F.1    Friedmann, J.A.2    DeGroot, J.3    Mehl, J.W.4
  • 56
    • 0014386609 scopus 로고
    • Studies on bovine factor X. II. Characterization of purified factor X. Observations on some alterations in zone electrophoretic and chromatographic behavior occurring during purification
    • Jackson, C. M., and Hanahan, D. J. (1968) Studies on bovine factor X. II. Characterization of purified factor X. Observations on some alterations in zone electrophoretic and chromatographic behavior occurring during purification. Biochemistry 7, 4506-4517
    • (1968) Biochemistry , vol.7 , pp. 4506-4517
    • Jackson, C.M.1    Hanahan, D.J.2
  • 57
    • 0015502153 scopus 로고
    • The purification and properties of activated factor X. Bovine factor X activated with Russell's viper venom
    • Radcliffe, R. D., and Barton, P. G. (1972) The purification and properties of activated factor X. Bovine factor X activated with Russell's viper venom. J. Biol. Chem. 247, 7735-7742
    • (1972) J. Biol. Chem. , vol.247 , pp. 7735-7742
    • Radcliffe, R.D.1    Barton, P.G.2
  • 58
    • 84857261516 scopus 로고    scopus 로고
    • The presentations of factor Xa and thrombin under flow
    • Haynes, L. M., Dubief, Y. C., and Mann, K. G. (2011) The presentations of factor Xa and thrombin under flow. J. Thromb. Haemost. 9, 346
    • (2011) J. Thromb. Haemost. , vol.9 , pp. 346
    • Haynes, L.M.1    Dubief, Y.C.2    Mann, K.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.