메뉴 건너뛰기




Volumn 90, Issue 3, 2003, Pages 385-397

Anti-heavy-chain monoclonal antibodies directed to the acidic regions of the factor VIII molecule inhibit the binding of factor VIII to phospholipids and von Willebrand factor

Author keywords

Epitope; Factor VIII; Monoclonal antibody; Phospholipid; VWF

Indexed keywords

BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 8; BLOOD CLOTTING FACTOR 8 ANTIBODY; GLUTATHIONE TRANSFERASE; HEAVY CHAIN MONOCLONAL ANTIBODY; IMMUNOGLOBULIN F(AB')2 FRAGMENT; IMMUNOGLOBULIN HEAVY CHAIN; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY F26F6; MONOCLONAL ANTIBODY F7B4; PHOSPHOLIPID; THROMBIN; UNCLASSIFIED DRUG; VON WILLEBRAND FACTOR;

EID: 0141429044     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/th02-09-0086     Document Type: Article
Times cited : (16)

References (51)
  • 1
    • 0027473752 scopus 로고
    • Recombinant factor VIII for the treatment of previously untreated patients with haemophilia A
    • Lusher JM, Arkin S, Abildgaard CF, Schwartz RS. Kogenate Previously Untreated Patient Study Group. Recombinant factor VIII for the treatment of previously untreated patients with haemophilia A. New Eng J Med 1993; 238: 453-9.
    • (1993) New Eng J Med , vol.238 , pp. 453-459
    • Lusher, J.M.1    Arkin, S.2    Abildgaard, C.F.3    Schwartz, R.S.4
  • 3
    • 0031048881 scopus 로고    scopus 로고
    • FVIII inhibitors in previously treated haemophilia A patients with a double virus-inactivated plasma derived factor VIII concentrate
    • Peerlinck K, Arnout J, Giambattista MD, et al. FVIII inhibitors in previously treated haemophilia A patients with a double virus-inactivated plasma derived factor VIII concentrate. Thromb Haemost 1997; 77: 80-6.
    • (1997) Thromb Haemost , vol.77 , pp. 80-86
    • Peerlinck, K.1    Arnout, J.2    Giambattista, M.D.3
  • 4
    • 0031726179 scopus 로고    scopus 로고
    • Modification of FVIII in therapeutic concentrates after virus inactivation by solvent-detergent and pasteurisation
    • Raut S, Di Giambattista M, Bevan SA, et al. Modification of FVIII in therapeutic concentrates after virus inactivation by solvent-detergent and pasteurisation. Thromb Haemost 1998; 80: 624-31.
    • (1998) Thromb Haemost , vol.80 , pp. 624-631
    • Raut, S.1    Di Giambattista, M.2    Bevan, S.A.3
  • 5
    • 0028266130 scopus 로고
    • A multicentre study of recombinant factor VIII (Recombinate): Safety, efficacy and inhibitor risk in previously untreated patients with haemophilia A
    • Bray GL, Gomperts ED, Courter S, et al. the Recombinate Study Group. A multicentre study of recombinant factor VIII (Recombinate): Safety, efficacy and inhibitor risk in previously untreated patients with haemophilia A. Blood 1994; 83: 2428-35.
    • (1994) Blood , vol.83 , pp. 2428-2435
    • Bray, G.L.1    Gomperts, E.D.2    Courter, S.3
  • 6
    • 0024328077 scopus 로고
    • Molecular basis of factor VIII inhibition by human antibodies. Antibodies that bind to the factor VIII light chain prevent the interaction of factor VIII with phospholipid
    • Arai M, Scandella D, Hoyer LW. Molecular basis of factor VIII inhibition by human antibodies. Antibodies that bind to the factor VIII light chain prevent the interaction of factor VIII with phospholipid. J Clin Invest 1989; 83: 1978-84.
    • (1989) J Clin Invest , vol.83 , pp. 1978-1984
    • Arai, M.1    Scandella, D.2    Hoyer, L.W.3
  • 7
    • 0027457180 scopus 로고
    • A factor VIII neutralizing monoclonal antibody and a human inhibitor alloantibody recognizing epitopes in the C2 domain inhibit factor VIII binding to von Willebrand factor and to phosphatidylserine
    • Shima M, Scandella D, Yoshioka A, et al. A factor VIII neutralizing monoclonal antibody and a human inhibitor alloantibody recognizing epitopes in the C2 domain inhibit factor VIII binding to von Willebrand factor and to phosphatidylserine. Thromb Haemost 1993; 69: 240-6.
    • (1993) Thromb Haemost , vol.69 , pp. 240-246
    • Shima, M.1    Scandella, D.2    Yoshioka, A.3
  • 8
    • 0029670912 scopus 로고    scopus 로고
    • The sequence Glu1811-Lys1818 of human blood coagulation factor VIII comprises a binding site for activated factor IX
    • Lenting PJ, Van De Loo JWP, Donath MJSH, et al. The sequence Glu1811-Lys1818 of human blood coagulation factor VIII comprises a binding site for activated factor IX. J Biol Chem 1996; 271: 1935-40.
    • (1996) J Biol Chem , vol.271 , pp. 1935-1940
    • Lenting, P.J.1    Van De Loo, J.W.P.2    Donath, M.J.S.H.3
  • 9
    • 0032127414 scopus 로고    scopus 로고
    • Some human inhibitor antibodies interfere with factor VIII binding to factor IX
    • Zhong D, Saenko EL, Shima M, et al. Some human inhibitor antibodies interfere with factor VIII binding to factor IX. Blood 1998; 92: 136-42.
    • (1998) Blood , vol.92 , pp. 136-142
    • Zhong, D.1    Saenko, E.L.2    Shima, M.3
  • 10
    • 0032055152 scopus 로고    scopus 로고
    • A human alloantibody interferes with binding of factor IXa to the factor VIII light chain
    • Fijnvandraat K, Celie PH, Turenhout EAM, et al. A human alloantibody interferes with binding of factor IXa to the factor VIII light chain. Blood 1998; 91: 2347-52.
    • (1998) Blood , vol.91 , pp. 2347-2352
    • Fijnvandraat, K.1    Celie, P.H.2    Turenhout, E.A.M.3
  • 11
    • 0028263884 scopus 로고
    • Inhibition of human factor VIIIa by anti-A2 subunit antibodies
    • Lollar P, Parker ET, Curtis JE, et al. Inhibition of human factor VIIIa by anti-A2 subunit antibodies. J Clin Invest 1994; 93: 2497-504.
    • (1994) J Clin Invest , vol.93 , pp. 2497-2504
    • Lollar, P.1    Parker, E.T.2    Curtis, J.E.3
  • 12
    • 0033570089 scopus 로고    scopus 로고
    • Human inhibitor antibodies specific for the factor VIII A2 domain disrupt the interaction between the subunit and factor IXa
    • Fay PJ, Scandella D. Human inhibitor antibodies specific for the factor VIII A2 domain disrupt the interaction between the subunit and factor IXa. J Biol Chem 1999; 274: 29826-30.
    • (1999) J Biol Chem , vol.274 , pp. 29826-29830
    • Fay, P.J.1    Scandella, D.2
  • 13
    • 20244363765 scopus 로고    scopus 로고
    • Catalytic activity of antibodies against factor VIII in patients with hemophilia A
    • Lacroix-Desmazes S, Moreau A, Sooryanarayana-Bonnemain C, et al. Catalytic activity of antibodies against factor VIII in patients with hemophilia A. Nat Med 1999; 5: 1044-7.
    • (1999) Nat Med , vol.5 , pp. 1044-1047
    • Lacroix-Desmazes, S.1    Moreau, A.2    Sooryanarayana-Bonnemain, C.3
  • 16
    • 0029154988 scopus 로고
    • Some factor VIII inhibitor antibodies recognize a common epitope corresponding to C2 domain amino acids 2248 through 2312, which overlap a phospholipid-binding site
    • Scandella D, Gilbert GE, Shima M, et al. Some factor VIII inhibitor antibodies recognize a common epitope corresponding to C2 domain amino acids 2248 through 2312, which overlap a phospholipid-binding site. Blood 1995; 86: 1811-9.
    • (1995) Blood , vol.86 , pp. 1811-1819
    • Scandella, D.1    Gilbert, G.E.2    Shima, M.3
  • 17
    • 0030926974 scopus 로고    scopus 로고
    • The inhibitor antibody response is more complex in hemophilia A patients than in most nonhemophiliacs with factor VIII autoantibodies
    • Prescott R, Nakai H, Saenko EL, et al. The inhibitor antibody response is more complex in hemophilia A patients than in most nonhemophiliacs with factor VIII autoantibodies. Blood 1998; 89: 3663-71.
    • (1997) Blood , vol.89 , pp. 3663-3671
    • Prescott, R.1    Nakai, H.2    Saenko, E.L.3
  • 18
    • 0023922071 scopus 로고
    • An immunogenic region within the val1670-glu1684 of the factor VIII light chain induces antibodies which inhibit binding of factor VIII to von Willebrand Factor
    • Foster PA, Fulcher CA, Houghten RA, et al. An immunogenic region within the val1670-glu1684 of the factor VIII light chain induces antibodies which inhibit binding of factor VIII to von Willebrand Factor. J Biol Chem 1988; 263: 5230-4.
    • (1988) J Biol Chem , vol.263 , pp. 5230-5234
    • Foster, P.A.1    Fulcher, C.A.2    Houghten, R.A.3
  • 19
    • 0034651022 scopus 로고    scopus 로고
    • Reduction of the antigenicity of factor VIII toward complex inhibitory antibody plasmas using multiply-substituted hybrid human/porcine factor VIII molecules
    • Barrow RT, Healey JF, Gailani D, et al. Reduction of the antigenicity of factor VIII toward complex inhibitory antibody plasmas using multiply-substituted hybrid human/porcine factor VIII molecules. Blood 2000; 95: 564-8.
    • (2000) Blood , vol.95 , pp. 564-568
    • Barrow, R.T.1    Healey, J.F.2    Gailani, D.3
  • 20
    • 0034661563 scopus 로고    scopus 로고
    • Molecular analysis of human anti-factor VIII antibodies by V gene phage display identifies a new epitope in the acidic region following the A2 domain
    • Van Den Brink EN, Turenhout EAM, Bank CMC, et al. Molecular analysis of human anti-factor VIII antibodies by V gene phage display identifies a new epitope in the acidic region following the A2 domain. Blood 2000; 96: 540-5.
    • (2000) Blood , vol.96 , pp. 540-545
    • Van Den Brink, E.N.1    Turenhout, E.A.M.2    Bank, C.M.C.3
  • 21
    • 0030903424 scopus 로고    scopus 로고
    • Molecular model for the triplicated A domains of human factor VIII based on the crystal structure of human ceruloplasmin
    • Pemberton S, Lindley P, Zaitsev V, et al. Molecular model for the triplicated A domains of human factor VIII based on the crystal structure of human ceruloplasmin. Blood 1997; 89: 2413-21.
    • (1997) Blood , vol.89 , pp. 2413-2421
    • Pemberton, S.1    Lindley, P.2    Zaitsev, V.3
  • 22
    • 0031804517 scopus 로고    scopus 로고
    • The factor VIII structure and mutation resource site: HAMSTeRS version 4
    • Kemball-Cook G, Tuddenham EG, Wacey AI. The factor VIII structure and mutation resource site: HAMSTeRS version 4. Nucleic Acids Res 1998; 26(1): 216-9.
    • (1998) Nucleic Acids Res , vol.26 , Issue.1 , pp. 216-219
    • Kemball-Cook, G.1    Tuddenham, E.G.2    Wacey, A.I.3
  • 23
    • 0037082464 scopus 로고    scopus 로고
    • 3-Dimensional structure of membrane-bound coagulation factor VIII: Modelling of the factor VIII heterodimer within a 3-dimensional density map derived by electron crystallography
    • Stoilova-McPhie S, Villoutreix BO, Mertens K, et al. 3-Dimensional structure of membrane-bound coagulation factor VIII: Modelling of the factor VIII heterodimer within a 3-dimensional density map derived by electron crystallography. Blood 2002; 99: 1215-23.
    • (2002) Blood , vol.99 , pp. 1215-1223
    • Stoilova-McPhie, S.1    Villoutreix, B.O.2    Mertens, K.3
  • 24
    • 0027488655 scopus 로고
    • Anti-factor VIII antibodies of hemophiliac patients are frequently directed towards nonfunctional determinants and do not exhibit isotypic restriction
    • Gilles JG, Arnout J, Vermylen J, et al. Anti-factor VIII antibodies of hemophiliac patients are frequently directed towards nonfunctional determinants and do not exhibit isotypic restriction Blood 1993; 82: 2452-61.
    • (1993) Blood , vol.82 , pp. 2452-2461
    • Gilles, J.G.1    Arnout, J.2    Vermylen, J.3
  • 25
    • 0022556050 scopus 로고
    • Preparation of F(ab′)2 fragments from mouse IgG of various subclasses
    • Lamoyi E. Preparation of F(ab′)2 fragments from mouse IgG of various subclasses. Methods Enzymol 1986; 121: 652-63.
    • (1986) Methods Enzymol , vol.121 , pp. 652-663
    • Lamoyi, E.1
  • 26
    • 0030055414 scopus 로고    scopus 로고
    • Evaluation of the fibrin binding profile of two anti-fibrin monoclonal antibodies
    • Raut S, Gaffney PJ. Evaluation of the fibrin binding profile of two anti-fibrin monoclonal antibodies. Thromb Haemost 1996; 76: 56-64.
    • (1996) Thromb Haemost , vol.76 , pp. 56-64
    • Raut, S.1    Gaffney, P.J.2
  • 27
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulphate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H, Von Jagow G. Tricine-sodium dodecyl sulphate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 1987; 166: 368-79.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 28
    • 0030571038 scopus 로고    scopus 로고
    • Comparison of three chemiluminescent horseradish peroxidase substrates for immunoblotting
    • Mattson DL, Bellehumeur TG. Comparison of three chemiluminescent horseradish peroxidase substrates for immunoblotting. Anal Biochem 1996; 240 (2): 306-8.
    • (1996) Anal Biochem , vol.240 , Issue.2 , pp. 306-308
    • Mattson, D.L.1    Bellehumeur, T.G.2
  • 29
    • 0033962015 scopus 로고    scopus 로고
    • A human antibody directed to the factor VIII C1 domain inhibits factor VIII cofactor activity and binding to von Willebrand factor
    • Jacquemin M, Benhida A, Peerlinck K, et al. A human antibody directed to the factor VIII C1 domain inhibits factor VIII cofactor activity and binding to von Willebrand factor. Blood 2000; 95: 156-63.
    • (2000) Blood , vol.95 , pp. 156-163
    • Jacquemin, M.1    Benhida, A.2    Peerlinck, K.3
  • 30
    • 0032528496 scopus 로고    scopus 로고
    • Mechanism and kinetics of factor VIII inactivation: Study with an IgG4 monoclonal antibody derived from a hemophilia A patient with inhibitor
    • Jacquemin MG, Desqueper BG, Benhida A, et al. Mechanism and kinetics of factor VIII inactivation: Study with an IgG4 monoclonal antibody derived from a hemophilia A patient with inhibitor. Blood 1998; 92: 496-506.
    • (1998) Blood , vol.92 , pp. 496-506
    • Jacquemin, M.G.1    Desqueper, B.G.2    Benhida, A.3
  • 31
    • 0026656122 scopus 로고
    • Spot synthesis: An easy technique for the positionally addressable, parallel chemical synthesis on a membrane support
    • Frank R. Spot synthesis: An easy technique for the positionally addressable, parallel chemical synthesis on a membrane support. Tetrahedron 1992; 48: 9217-32.
    • (1992) Tetrahedron , vol.48 , pp. 9217-9232
    • Frank, R.1
  • 32
    • 0030152613 scopus 로고    scopus 로고
    • Improved performances of spot multiple peptide synthesis
    • Molina F, Laune D, Gougat C, et al. Improved performances of spot multiple peptide synthesis. Peptide Res 1996; 9: 151-5.
    • (1996) Peptide Res , vol.9 , pp. 151-155
    • Molina, F.1    Laune, D.2    Gougat, C.3
  • 33
    • 0026952154 scopus 로고
    • Automated multiple peptide synthesis
    • Gausepohl H, Boulin C, Kraft M, et al. Automated multiple peptide synthesis. Peptide Res 1992; 5: 315-20.
    • (1992) Peptide Res , vol.5 , pp. 315-320
    • Gausepohl, H.1    Boulin, C.2    Kraft, M.3
  • 34
    • 0028837315 scopus 로고
    • The Nijmegen modification of the Bethesda Assay for factor VIII:C inhibitors: Improved specificity and reliability
    • Verbruggen B, Novakova I, Wessels H, et al. The Nijmegen modification of the Bethesda Assay for factor VIII:C inhibitors: Improved specificity and reliability. Thromb Haemost 1995; 73: 247-51.
    • (1995) Thromb Haemost , vol.73 , pp. 247-251
    • Verbruggen, B.1    Novakova, I.2    Wessels, H.3
  • 35
    • 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(1): 93-100.
    • (2001) Thromb Haemost , vol.85 , Issue.1 , pp. 93-100
    • Sandberg, H.1    Almstedt, A.2    Brandt, J.3
  • 36
    • 0036277634 scopus 로고    scopus 로고
    • Activation profiles of FVIII in concentrates reflect one-stage/chromogenic potency discrepancies
    • Hubbard AR, Weller L, Bevan SA. Activation profiles of FVIII in concentrates reflect one-stage/chromogenic potency discrepancies. Br J Haematol 2002; 117: 957-60.
    • (2002) Br J Haematol , vol.117 , pp. 957-960
    • Hubbard, A.R.1    Weller, L.2    Bevan, S.A.3
  • 37
    • 0027208124 scopus 로고
    • The behaviour of different factor VIII concentrates in a chromogenic factor X-activating system
    • Kemball-Cook G, Tubbs JE, Dawson NJ, et al. The behaviour of different factor VIII concentrates in a chromogenic factor X-activating system. Br J Haematol 1993; 84: 273-8.
    • (1993) Br J Haematol , vol.84 , pp. 273-278
    • Kemball-Cook, G.1    Tubbs, J.E.2    Dawson, N.J.3
  • 38
    • 0023625307 scopus 로고
    • The interaction of rDNA factor VIII, factordes-797-1562 and factordes-797-1562-derived peptides with phospholipid
    • Bloom JW. The interaction of rDNA factor VIII, factordes-797-1562 and factordes-797-1562-derived peptides with phospholipid. Thromb Res 1987; 48: 439-48.
    • (1987) Thromb Res , vol.48 , pp. 439-448
    • Bloom, J.W.1
  • 39
    • 0032750777 scopus 로고    scopus 로고
    • Phospholipid binding of factor VIII in different therapeutic concentrates
    • Raut S, Weller L, Barrowcliffe TW. Phospholipid binding of factor VIII in different therapeutic concentrates. Br J Haematol 1999; 107: 323-9.
    • (1999) Br J Haematol , vol.107 , pp. 323-329
    • Raut, S.1    Weller, L.2    Barrowcliffe, T.W.3
  • 40
    • 0021984522 scopus 로고
    • Human factor VIII procoagulant protein. Monoclonal antibodies define precursor-product relationships and functional epitopes
    • Fulcher CA, Roberts JR, Holland LZ, et al. Human factor VIII procoagulant protein. Monoclonal antibodies define precursor-product relationships and functional epitopes. J Clin Invest 1985; 76: 117-24.
    • (1985) J Clin Invest , vol.76 , pp. 117-124
    • Fulcher, C.A.1    Roberts, J.R.2    Holland, L.Z.3
  • 41
    • 0021677942 scopus 로고
    • Structure of human factor VIII
    • Vehar GA, Keyt B, Eaton D, et al. Structure of human factor VIII. Nature 1984; 312: 337-42.
    • (1984) Nature , vol.312 , pp. 337-342
    • Vehar, G.A.1    Keyt, B.2    Eaton, D.3
  • 42
    • 0021715168 scopus 로고
    • Expression of active human factor VIII from recombinant DNA clones
    • Wood WI, Capon DJ, Simonsen CC, et al. Expression of active human factor VIII from recombinant DNA clones. Nature 1984; 312: 330-7.
    • (1984) Nature , vol.312 , pp. 330-337
    • Wood, W.I.1    Capon, D.J.2    Simonsen, C.C.3
  • 43
    • 0027295497 scopus 로고
    • Role of the COOH-terminal acidic region of A1 subunit in A2 subunit retention in human factor VIIIa
    • Fay PJ, Haidaris PJ, Huggins CF. Role of the COOH-terminal acidic region of A1 subunit in A2 subunit retention in human factor VIIIa. J Biol Chem 1993; 268: 17861-6.
    • (1993) J Biol Chem , vol.268 , pp. 17861-17866
    • Fay, P.J.1    Haidaris, P.J.2    Huggins, C.F.3
  • 44
    • 0031027575 scopus 로고    scopus 로고
    • Localization of a factor X interactive site in the A1 subunit of factor VIIIa
    • Lapan KA, Fay PJ. Localization of a factor X interactive site in the A1 subunit of factor VIIIa. J Biol Chem 1997; 272: 2082-8.
    • (1997) J Biol Chem , vol.272 , pp. 2082-2088
    • Lapan, K.A.1    Fay, P.J.2
  • 45
    • 0025297357 scopus 로고
    • Synthetic factor VIII peptides with amino acid sequences contained within the C2 domain of factor VIII inhibit factor VIII binding to phosphatidylserine
    • Foster PA, Fulcher CA, Houghten RA, et al. Synthetic factor VIII peptides with amino acid sequences contained within the C2 domain of factor VIII inhibit factor VIII binding to phosphatidylserine. Blood 1990; 75 (10): 1999-2004.
    • (1990) Blood , vol.75 , Issue.10 , pp. 1999-2004
    • Foster, P.A.1    Fulcher, C.A.2    Houghten, R.A.3
  • 46
    • 0033579442 scopus 로고    scopus 로고
    • Electron crystallography of human blood coagulation factor VIII bound to phospholipid monolayers
    • Stoylova SS, Lenting PJ, Kemball-Cook G, et al. Electron crystallography of human blood coagulation factor VIII bound to phospholipid monolayers. J Biol Chem 1999; 274: 36573-8.
    • (1999) J Biol Chem , vol.274 , pp. 36573-36578
    • Stoylova, S.S.1    Lenting, P.J.2    Kemball-Cook, G.3
  • 47
    • 1842408993 scopus 로고
    • Proteolytic requirements for thrombin activation of anti-hemophilic factor (factor VIII)
    • Pittman DD, Kaufman RJ. Proteolytic requirements for thrombin activation of anti-hemophilic factor (factor VIII). Proc Natl Acad Sci USA 1988; 85: 2429-33.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2429-2433
    • Pittman, D.D.1    Kaufman, R.J.2
  • 48
    • 0029833923 scopus 로고    scopus 로고
    • Kinetics of factor VIII light-chain cleavage by thrombin and factor Xa. A regulatory role of the factor VIII heavy-chain region Lys713-Arg740
    • Donath MJ, Lenting PJ, Van-Mourik JA, et al. Kinetics of factor VIII light-chain cleavage by thrombin and factor Xa. A regulatory role of the factor VIII heavy-chain region Lys713-Arg740. Eur J Biochem 1996; 240: 365-72.
    • (1996) Eur J Biochem , vol.240 , pp. 365-372
    • Donath, M.J.1    Lenting, P.J.2    Van-Mourik, J.A.3
  • 49
    • 0034913420 scopus 로고    scopus 로고
    • Influence of von Willebrand factor on the reactivity of human factor VIII inhibitors with factor VIII
    • Gensana M, Altisent C, Aznar JA, et al. Influence of von Willebrand factor on the reactivity of human factor VIII inhibitors with factor VIII. Haemophilia 2001; 7 (4): 369-74.
    • (2001) Haemophilia , vol.7 , Issue.4 , pp. 369-374
    • Gensana, M.1    Altisent, C.2    Aznar, J.A.3
  • 50
    • 0023274887 scopus 로고
    • The effect of thrombin on the complex between factor VIII and von Willebrand factor
    • Hamer RJ, Koedam JA, Beeser-Visser NH, et al. The effect of thrombin on the complex between factor VIII and von Willebrand factor. Eur J Biochem 1987; 167 (2): 253-9.
    • (1987) Eur J Biochem , vol.167 , Issue.2 , pp. 253-259
    • Hamer, R.J.1    Koedam, J.A.2    Beeser-Visser, N.H.3
  • 51
    • 0023918416 scopus 로고
    • Reconstitution of human factor VIII from isolated subunits
    • Fay PJ. Reconstitution of human factor VIII from isolated subunits. Arch Biochem Biophys 1988; 262 (2): 525-31.
    • (1988) Arch Biochem Biophys , vol.262 , Issue.2 , pp. 525-531
    • Fay, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.