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Volumn 15, Issue 1, 2009, Pages 63-72

Potency and mass of factor VIII in FVIII products

Author keywords

Factor VIII activity; Factor VIII antigen; Factor VIII products; Intrinsic factor Xase; Thrombin generation; Tissue factor

Indexed keywords

BLOOD CLOTTING FACTOR 8; RECOMBINANT BLOOD CLOTTING FACTOR 8;

EID: 63049114058     PISSN: 13518216     EISSN: 13652516     Source Type: Journal    
DOI: 10.1111/j.1365-2516.2008.01826.x     Document Type: Article
Times cited : (20)

References (40)
  • 2
    • 0000702696 scopus 로고
    • A concentrate of human antihaemophilic factor - Its use in six cases of haemophilia
    • Kekwick RA, Wolf P. A concentrate of human antihaemophilic factor -its use in six cases of haemophilia. Lancet 1957; i: 647.
    • (1957) Lancet , vol.1 , pp. 647
    • Kekwick, R.A.1    Wolf, P.2
  • 3
    • 0014673283 scopus 로고
    • Treatment of hemophilia B with a new clotting-factor concentrate
    • Hoag MS, Johnson FF, Robinson JA, Aggeler PM. Treatment of hemophilia B with a new clotting-factor concentrate. N Engl J Med 1969; 28: 581-6.
    • (1969) N Engl J Med , vol.28 , pp. 581-586
    • Hoag, M.S.1    Johnson, F.F.2    Robinson, J.A.3    Aggeler, P.M.4
  • 4
    • 0021141488 scopus 로고
    • Hepatitis, epidemiology and liver function in hemophiliacs in Sweden
    • Schulman S, Wiechel B. Hepatitis, epidemiology and liver function in hemophiliacs in Sweden. Acta Med Scand 1984; 215: 249-56.
    • (1984) Acta Med Scand , vol.215 , pp. 249-256
    • Schulman, S.1    Wiechel, B.2
  • 5
    • 0027411861 scopus 로고
    • Factor IX concentrates for clinical use
    • Thompson AR. Factor IX concentrates for clinical use. Semin Thromb Hemost 1993; 19: 25-36.
    • (1993) Semin Thromb Hemost , vol.19 , pp. 25-36
    • Thompson, A.R.1
  • 6
    • 0035098164 scopus 로고    scopus 로고
    • Effects of HIV infection on age and cause of death for persons with hemophilia A in the United States
    • Chorba TL, Holman RC, Clarke MJ, Evatt BL. Effects of HIV infection on age and cause of death for persons with hemophilia A in the United States. Am J Hematol 2001; 66: 229-40.
    • (2001) Am J Hematol , vol.66 , pp. 229-240
    • Chorba, T.L.1    Holman, R.C.2    Clarke, M.J.3    Evatt, B.L.4
  • 7
    • 1642595858 scopus 로고
    • Characterization of the human factor VIII procoagulant protein with a heterologous precipitating antibody
    • Fulcher CA, Zimmerman TS. Characterization of the human factor VIII procoagulant protein with a heterologous precipitating antibody. Proc Natl Acad Sci USA 1982; 79: 1648-52.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 1648-1652
    • Fulcher, C.A.1    Zimmerman, T.S.2
  • 8
    • 0022965446 scopus 로고
    • Characterization of four monoclonal antibodies to factor VIII coagulant protein and their use in immunopurification of factor VIII
    • Croissant MP, van de Pol H, Lee HH, Allain JP. Characterization of four monoclonal antibodies to factor VIII coagulant protein and their use in immunopurification of factor VIII. Thromb Haemost 1986; 56: 271-6.
    • (1986) Thromb Haemost , vol.56 , pp. 271-276
    • Croissant, M.P.1    van de Pol, H.2    Lee, H.H.3    Allain, J.P.4
  • 9
    • 0025644310 scopus 로고
    • Human recombinant DNA-derived antihemophilic factor (factor VIII) in the treatment of hemophilia A. Recombinant Factor VIII Study Group
    • Schwartz RS, Abildgaard CF, Aledort LM et al. Human recombinant DNA-derived antihemophilic factor (factor VIII) in the treatment of hemophilia A. Recombinant Factor VIII Study Group. N Engl J Med 1990; 323: 1800-5.
    • (1990) N Engl J Med , vol.323 , pp. 1800-1805
    • Schwartz, R.S.1    Abildgaard, C.F.2    Aledort, L.M.3
  • 10
    • 0035159198 scopus 로고    scopus 로고
    • Structural and functional characteristics of the B-domain-deleted recombinant factor VIII protein, r-VIII SQ
    • Sandberg H, Almstedt A, Brandt J et al. Structural and functional characteristics of the B-domain-deleted recombinant factor VIII protein, r-VIII SQ. Thromb Haemost 2001; 85: 93-100.
    • (2001) Thromb Haemost , vol.85 , pp. 93-100
    • Sandberg, H.1    Almstedt, A.2    Brandt, J.3
  • 12
    • 0036017374 scopus 로고    scopus 로고
    • First and second generation recombinant factor VIII concentrates in previously untreated patients: Recovery, safety, efficacy, and inhibitor development
    • Lusher JM. First and second generation recombinant factor VIII concentrates in previously untreated patients: Recovery, safety, efficacy, and inhibitor development. Semin Thromb Haemost 2002; 28: 273-6.
    • (2002) Semin Thromb Haemost , vol.28 , pp. 273-276
    • Lusher, J.M.1
  • 13
    • 0036017373 scopus 로고    scopus 로고
    • First and next generation native rFVIII in the treatment of hemophilia A. What has been achieved? Can patients be switched safely?
    • Suiter TM. First and next generation native rFVIII in the treatment of hemophilia A. What has been achieved? Can patients be switched safely? Semin Thromb Haemost 2002; 28: 278-83.
    • (2002) Semin Thromb Haemost , vol.28 , pp. 278-283
    • Suiter, T.M.1
  • 14
    • 33646158848 scopus 로고    scopus 로고
    • The economics of haemophilia treatments
    • In: Lee CH, Berntorp EE, Hoots KW, eds. Malden, MA: Blackwell Publishing
    • Miners AH. The economics of haemophilia treatments. In: Lee CH, Berntorp EE, Hoots KW, eds. Textbook of Hermophilia. Malden, MA: Blackwell Publishing, 2005: 351-8.
    • (2005) Textbook of Hermophilia , pp. 351-358
    • Miners, A.H.1
  • 15
    • 34447121601 scopus 로고    scopus 로고
    • Products used to treat hemophilia
    • In: Lee CH, Berntorp EE, Hoots KW, eds. Malden, MA: Blackwell Publishing
    • Barrowcliffe TW. Products used to treat hemophilia. In: Lee CH, Berntorp EE, Hoots KW, eds. Textbook of Hermophilia. Malden, MA: Blackwell Publishing, 2005: 242-8.
    • (2005) Textbook of Hermophilia , pp. 242-248
    • Barrowcliffe, T.W.1
  • 16
    • 0032877592 scopus 로고    scopus 로고
    • Determination of coagulation factor VIII activity by a chromogenic substrate method on STA, an automated coagulation analyzer
    • Kleinveld HA, Andersson NE, van Voorthuiozen H, den Hartog J, de Groot PG. Determination of coagulation factor VIII activity by a chromogenic substrate method on STA, an automated coagulation analyzer. Scand J Clin Invest 1999; 59: 335-41.
    • (1999) Scand J Clin Invest , vol.59 , pp. 335-341
    • Kleinveld, H.A.1    Andersson, N.E.2    van Voorthuiozen, H.3    den Hartog, J.4    de Groot, P.G.5
  • 17
    • 0034952586 scopus 로고    scopus 로고
    • Measurement of factor VIII activity of B-domain deleted recombinant factor VIII
    • Mikaelsson M, Oswaldsson U, Jankowski MA. Measurement of factor VIII activity of B-domain deleted recombinant factor VIII. Semin Hematol 2001; 2 (Suppl. 4): 13-23.
    • (2001) Semin Hematol , vol.2 , Issue.SUPPL. 4 , pp. 13-23
    • Mikaelsson, M.1    Oswaldsson, U.2    Jankowski, M.A.3
  • 18
    • 0036017368 scopus 로고    scopus 로고
    • Coagulation and chromogenic assays of factor VIII activity: General aspects, standardization, and recommendations
    • Barrowcliffe TW, Raut S, Sands D, Hubbard AR. Coagulation and chromogenic assays of factor VIII activity: General aspects, standardization, and recommendations. Semin Thromb Haemost 2002; 28: 247-55.
    • (2002) Semin Thromb Haemost , vol.28 , pp. 247-255
    • Barrowcliffe, T.W.1    Raut, S.2    Sands, D.3    Hubbard, A.R.4
  • 19
    • 0036017369 scopus 로고    scopus 로고
    • Assaying the circulating factor VIII activity in hemophilia A patients treated with recombinant factor VIII products
    • Mikaelsson M, Oswaldsson U. Assaying the circulating factor VIII activity in hemophilia A patients treated with recombinant factor VIII products. Semin Thromb Haemost 2002; 28: 257-64.
    • (2002) Semin Thromb Haemost , vol.28 , pp. 257-264
    • Mikaelsson, M.1    Oswaldsson, U.2
  • 20
    • 0031857499 scopus 로고    scopus 로고
    • In vivo recovery with products of very high purity - Assay discrepancies
    • Lusher JM, Hillman-Wiseman C, Hurst D. In vivo recovery with products of very high purity -assay discrepancies. Haemophilia 1998; 4: 641-5.
    • (1998) Haemophilia , vol.4 , pp. 641-645
    • Lusher, J.M.1    Hillman-Wiseman, C.2    Hurst, D.3
  • 21
    • 0031878077 scopus 로고    scopus 로고
    • Influence of phospholipids on the assessment of factor VIII activity
    • Mikaelsson M, Oswaldsson U, Sandberg H. Influence of phospholipids on the assessment of factor VIII activity. Haemophilia 1998; 4: 646-50.
    • (1998) Haemophilia , vol.4 , pp. 646-650
    • Mikaelsson, M.1    Oswaldsson, U.2    Sandberg, H.3
  • 22
    • 1842293383 scopus 로고    scopus 로고
    • Evaluation of the initiation phase of blood coagulation using ultrasensitive assays for serine proteases
    • Butenas S, van't Veer C, Mann KG. Evaluation of the initiation phase of blood coagulation using ultrasensitive assays for serine proteases. J Biol Chem 1997; 272: 21527-33.
    • (1997) J Biol Chem , vol.272 , pp. 21527-21533
    • Butenas, S.1    van't Veer, C.2    Mann, K.G.3
  • 23
    • 0028064839 scopus 로고
    • A model for the tissue factor pathway to thrombin. I. An empirical study
    • Lawson JH, Kalafatis M, Stram S, Mann KG. A model for the tissue factor pathway to thrombin. I. An empirical study. J Biol Chem 1994; 269: 23357-66.
    • (1994) J Biol Chem , vol.269 , pp. 23357-23366
    • Lawson, J.H.1    Kalafatis, M.2    Stram, S.3    Mann, K.G.4
  • 24
    • 0031058039 scopus 로고    scopus 로고
    • Regulation of tissue factor initiated thrombin generation by stoichiometric inhibitors tissue factor pathway inhibitor, antithrombin-III, and heparin cofactor-II
    • van 't Veer C, Mann KG. Regulation of tissue factor initiated thrombin generation by stoichiometric inhibitors tissue factor pathway inhibitor, antithrombin-III, and heparin cofactor-II. J Biol Chem 1997; 272: 4367-77.
    • (1997) J Biol Chem , vol.272 , pp. 4367-4377
    • van 't Veer, C.1    Mann, K.G.2
  • 26
    • 0019785751 scopus 로고
    • A simplified procedure for purification of human prothrombin, factor IX and factor X
    • Bajaj SP, Rapaport SI, Prodanos C. A simplified procedure for purification of human prothrombin, factor IX and factor X. Prep Biochem 1981; 11: 397-412.
    • (1981) Prep Biochem , vol.11 , pp. 397-412
    • Bajaj, S.P.1    Rapaport, S.I.2    Prodanos, C.3
  • 27
    • 0342300993 scopus 로고
    • Isolation of functional human coagulation factor V by using a hybridoma antibody
    • Katzmann JA, Nesheim ME, Hibbard LS, Mann KG. Isolation of functional human coagulation factor V by using a hybridoma antibody. Proc Natl Acad Sci USA 1981; 78: 162-6.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 162-166
    • Katzmann, J.A.1    Nesheim, M.E.2    Hibbard, L.S.3    Mann, K.G.4
  • 28
    • 0022003799 scopus 로고
    • Reactive site peptide structural similarity between heparin cofactor II and antithrombin III
    • Griffith MJ, Noyes CM, Church FC. Reactive site peptide structural similarity between heparin cofactor II and antithrombin III. J Biol Chem 1985; 260: 2218-25.
    • (1985) J Biol Chem , vol.260 , pp. 2218-2225
    • Griffith, M.J.1    Noyes, C.M.2    Church, F.C.3
  • 29
    • 57749188526 scopus 로고    scopus 로고
    • Determination of free sulfhydryls in human factor VIII
    • Kumar H, Healey JF, Lollar P, Durrani MJ. Determination of free sulfhydryls in human factor VIII. J Thromb Haemost 2003; 1 (Suppl. 1): P1067.
    • (2003) J Thromb Haemost , vol.1 , Issue.SUPPL. 1
    • Kumar, H.1    Healey, J.F.2    Lollar, P.3    Durrani, M.J.4
  • 31
    • 0020633335 scopus 로고
    • The interaction of bovine factor V and factor V-derived peptides with phospholipid vesicles
    • Higgins DL, Mann KG. The interaction of bovine factor V and factor V-derived peptides with phospholipid vesicles. J Biol Chem 1983; 258: 6503-8.
    • (1983) J Biol Chem , vol.258 , pp. 6503-6508
    • Higgins, D.L.1    Mann, K.G.2
  • 32
    • 0025833280 scopus 로고
    • A monoclonal antibody to factor VIII inhibits von Willebrand factor binding and thrombin cleavage
    • Precup JW, Kline BC, Fass DN. A monoclonal antibody to factor VIII inhibits von Willebrand factor binding and thrombin cleavage. Blood 1991; 77: 1929-36.
    • (1991) Blood , vol.77 , pp. 1929-1936
    • Precup, J.W.1    Kline, B.C.2    Fass, D.N.3
  • 33
    • 0022445266 scopus 로고
    • The size of human factor VIII heterodimers and the effects produced by thrombin
    • Fay PJ, Anderson MT, Chavin SI, Marder VJ. The size of human factor VIII heterodimers and the effects produced by thrombin. Biochim Biophys Acta 1986; 871: 268-78.
    • (1986) Biochim Biophys Acta , vol.871 , pp. 268-278
    • Fay, P.J.1    Anderson, M.T.2    Chavin, S.I.3    Marder, V.J.4
  • 34
    • 0019831499 scopus 로고
    • The role of phospholipid and factor VIIIa in the activation of bovine factor X
    • van Dieijen G, Tans G, Rosing J, Hemker HC. The role of phospholipid and factor VIIIa in the activation of bovine factor X. J Biol Chem 1981; 256: 3433-42.
    • (1981) J Biol Chem , vol.256 , pp. 3433-3442
    • van Dieijen, G.1    Tans, G.2    Rosing, J.3    Hemker, H.C.4
  • 36
    • 0037166290 scopus 로고    scopus 로고
    • A model for the stoichiometric regulation of blood coagulation
    • Hockin MF, Jones KC, Everse SJ, Mann KG. A model for the stoichiometric regulation of blood coagulation. J Biol Chem 2002; 277: 18322-33.
    • (2002) J Biol Chem , vol.277 , pp. 18322-18333
    • Hockin, M.F.1    Jones, K.C.2    Everse, S.J.3    Mann, K.G.4
  • 37
    • 0029941850 scopus 로고    scopus 로고
    • Comparison of activated protein C/protein S-mediated inactivation of human factor VIII and factor V
    • Lu D, Kalafatis M, Mann KG, Long GL. Comparison of activated protein C/ protein S-mediated inactivation of human factor VIII and factor V. Blood 1996; 87: 4708-17.
    • (1996) Blood , vol.87 , pp. 4708-4717
    • Lu, D.1    Kalafatis, M.2    Mann, K.G.3    Long, G.L.4
  • 38
    • 0030768937 scopus 로고    scopus 로고
    • Interaction of factor IXa with factor VIIIa. Effects of protease domain Ca2+ binding site, proteolysis in the autolysis loop, phospholipid, and factor X
    • Mathur A, Zhohg D, Sabharwal AK, Smith KJ, Bajaj SP. Interaction of factor IXa with factor VIIIa. Effects of protease domain Ca2+ binding site, proteolysis in the autolysis loop, phospholipid, and factor X. J Biol Chem 1997; 272: 23418-26.
    • (1997) J Biol Chem , vol.272 , pp. 23418-23426
    • Mathur, A.1    Zhohg, D.2    Sabharwal, A.K.3    Smith, K.J.4    Bajaj, S.P.5
  • 39
    • 0021252593 scopus 로고
    • Stabilization of thrombin-activated porcine factor VIII:C by factor IXa and phospholipid
    • Lollar P, Knutson GJ, Fass DN. Stabilization of thrombin-activated porcine factor VIII:C by factor IXa and phospholipid. Blood 1984; 63: 1303-8.
    • (1984) Blood , vol.63 , pp. 1303-1308
    • Lollar, P.1    Knutson, G.J.2    Fass, D.N.3
  • 40
    • 4844227035 scopus 로고    scopus 로고
    • Relationships between factor VIII: Ag and factor VIII in recombinant and plasma-derived factor VIII concentrates
    • Lin Y, Yang X, Chevrier M-C et al. Relationships between factor VIII: Ag and factor VIII in recombinant and plasma-derived factor VIII concentrates. Haemophilia 2004; 10: 459-69.
    • (2004) Haemophilia , vol.10 , pp. 459-469
    • Lin, Y.1    Yang, X.2    Chevrier, M.-C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.