메뉴 건너뛰기




Volumn 81, Issue 1, 1996, Pages 65-73

Localization of a calcium-dependent epitope to the amino terminal region of the Gla domain of human factor IX

Author keywords

Calcium dependent antibody; Epitope mapping; Factor IX

Indexed keywords

BLOOD CLOTTING FACTOR 9; CALCIUM; EPITOPE;

EID: 0030047256     PISSN: 00493848     EISSN: None     Source Type: Journal    
DOI: 10.1016/0049-3848(95)00214-6     Document Type: Article
Times cited : (6)

References (28)
  • 1
    • 0026337077 scopus 로고
    • The coagulation cascade: Initiation, maintenance, and regulation
    • DAVIE, E.W., FUJIKAWA, K. and KISIEL, W. The coagulation cascade: Initiation, maintenance, and regulation. Biochemistry 30, 10363-10370, 1991.
    • (1991) Biochemistry , vol.30 , pp. 10363-10370
    • Davie, E.W.1    Fujikawa, K.2    Kisiel, W.3
  • 2
    • 0020001023 scopus 로고
    • 2+ on the kinetic parameters of the activation of factor IX by factor XIa
    • 2+ on the kinetic parameters of the activation of factor IX by factor XIa. J. Biol. Chem. 257, 4127-4132, 1982.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4127-4132
    • Bajaj, S.P.1
  • 3
    • 0017138587 scopus 로고
    • Role of γ-carboxyglutamic acid: An unusal protein transition required for the calcium-dependent binding of prothrombin to phospholipid
    • NELSESTUEN, G.L. Role of γ-carboxyglutamic acid: An unusal protein transition required for the calcium-dependent binding of prothrombin to phospholipid. J. Biol. Chem. 251, 5648-5656, 1976.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5648-5656
    • Nelsestuen, G.L.1
  • 4
    • 0022297837 scopus 로고
    • Comparison of lipid binding and kinetic properties of normal, variant, and γ-carboxyglutamic acid modified human factor IX and factor IXa
    • JONES, M.E., GRIFFITH, M.J., MONROE, D.M., ROBERTS, H.R. and LENTZ, B.R. Comparison of lipid binding and kinetic properties of normal, variant, and γ-carboxyglutamic acid modified human factor IX and factor IXa. Biochemistry 24, 8064-8069, 1985.
    • (1985) Biochemistry , vol.24 , pp. 8064-8069
    • Jones, M.E.1    Griffith, M.J.2    Monroe, D.M.3    Roberts, H.R.4    Lentz, B.R.5
  • 5
    • 0023103151 scopus 로고
    • Molecular interactions of the intrinsic activation complex of coagulation: Binding of native and activated human factors IX and X to defined phospholipid vesicles
    • BURRI, B.J., EDGINGTON, T.S. and FAIR, D.S. Molecular interactions of the intrinsic activation complex of coagulation: binding of native and activated human factors IX and X to defined phospholipid vesicles. Biochim. Biophys. Acta 923, 176-186, 1987.
    • (1987) Biochim. Biophys. Acta , vol.923 , pp. 176-186
    • Burri, B.J.1    Edgington, T.S.2    Fair, D.S.3
  • 7
    • 0024358111 scopus 로고
    • Protein structural requirements and properties of membrane binding by γ-carboxyglutamic acid-containing plasma proteins and peptides
    • SCHWALBE, R.A., RYAN, J., STERN, D.M., KISIEL, W., DAHLBÄCK, B. and NELSESTUEN, G.L. Protein structural requirements and properties of membrane binding by γ-carboxyglutamic acid-containing plasma proteins and peptides. J. Biol. Chem. 264, 20288-20296, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20288-20296
    • Schwalbe, R.A.1    Ryan, J.2    Stern, D.M.3    Kisiel, W.4    Dahlbäck, B.5    Nelsestuen, G.L.6
  • 8
    • 0025317472 scopus 로고
    • Kinetics of coagulation factor X activation by platelet-bound factor IXa
    • RAWALA-SHEIKH, R., AHMAD, S.S., ASHBY, B. and WALSH, P.N. Kinetics of coagulation factor X activation by platelet-bound factor IXa. Biochemistry 29, 2606-2611, 1990.
    • (1990) Biochemistry , vol.29 , pp. 2606-2611
    • Rawala-Sheikh, R.1    Ahmad, S.S.2    Ashby, B.3    Walsh, P.N.4
  • 9
    • 0020631381 scopus 로고
    • Binding of coagulation factors IX and X to the endothelial cell surface
    • HEIMARK, R.L. and SCHWARTZ, S.M. Binding of coagulation factors IX and X to the endothelial cell surface. Biochem. Biophys. Res. Commun. 111, 723-731,1983.
    • (1983) Biochem. Biophys. Res. Commun. , vol.111 , pp. 723-731
    • Heimark, R.L.1    Schwartz, S.M.2
  • 11
    • 0026660188 scopus 로고
    • The binding of human factor IX to endothelial cells is mediated by residues 3-11
    • CHEUNG, W.-F., HAMAGUCHI, N., SMITH, K.J. and STAFFORD, D.W. The binding of human factor IX to endothelial cells is mediated by residues 3-11. J. Biol. Chem. 267, 20529-20531, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20529-20531
    • Cheung, W.-F.1    Hamaguchi, N.2    Smith, K.J.3    Stafford, D.W.4
  • 12
    • 0023664212 scopus 로고    scopus 로고
    • Mg(II) binding by bovine prothrombin fragment 1 via equilibrium dialysis and the relative roles of Mg(II) and ca(II) in blood coagulation
    • DEERFIELD, D.W., OLSON, D.L., BERKOWITZ, P., BYRD, P.A., KOEHLER, K.A., PEDERSEN, L.G. and HISKEY, R.G. Mg(II) binding by bovine prothrombin fragment 1 via equilibrium dialysis and the relative roles of Mg(II) and Ca(II) in Blood coagulation. J. Biol. Chem. 262, 4017-4023.
    • J. Biol. Chem. , vol.262 , pp. 4017-4023
    • Deerfield, D.W.1    Olson, D.L.2    Berkowitz, P.3    Byrd, P.A.4    Koehler, K.A.5    Pedersen, L.G.6    Hiskey, R.G.7
  • 14
    • 0023020122 scopus 로고
    • Prothrombin requires two sequential metal-dependent conformational transitions to bind phospholipid
    • BOROWSKI, M., FURIE, B.C., BAUMINGER, S. and FURIE, B. Prothrombin requires two sequential metal-dependent conformational transitions to bind phospholipid. J. Biol. Chem. 261, 14969-14975, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14969-14975
    • Borowski, M.1    Furie, B.C.2    Bauminger, S.3    Furie, B.4
  • 15
    • 0023239941 scopus 로고
    • The factor IX phospholipid-binding site is required for calcium-dependent activation of factor IX by factor XIa
    • LIEBMAN, H.A., FURIE, B.C. and FURIE, B. The factor IX phospholipid-binding site is required for calcium-dependent activation of factor IX by factor XIa. J. Biol. Chem. 262, 7605-7612, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7605-7612
    • Liebman, H.A.1    Furie, B.C.2    Furie, B.3
  • 16
    • 0025315868 scopus 로고
    • Anti-human factor IX monoclonal antibodies specific for calcium ion-induced conformations
    • SUGO, T., MIZUGUCHI, J., KAMIKUBO, Y. and MATSUDA, M. Anti-human factor IX monoclonal antibodies specific for calcium ion-induced conformations. Thromb. Res. 58, 603-614, 1990.
    • (1990) Thromb. Res. , vol.58 , pp. 603-614
    • Sugo, T.1    Mizuguchi, J.2    Kamikubo, Y.3    Matsuda, M.4
  • 17
    • 85031232783 scopus 로고    scopus 로고
    • Localization of a metal-dependent epitope to the amino terminal residues 33-40 of human factor IX
    • in press
    • CHEUNG, W.-F., WOLBERG, A.S., STAFFORD, D.W. and SMITH, K.J. Localization of a metal-dependent epitope to the amino terminal residues 33-40 of human factor IX. Thromb. Res. (in press).
    • Thromb. Res.
    • Cheung, W.-F.1    Wolberg, A.S.2    Stafford, D.W.3    Smith, K.J.4
  • 18
    • 0021365144 scopus 로고
    • Monoclonal antibodies to factor IX: Characterization and use in immunoassays for factor IX
    • SMITH, K.J. and ONO, K. Monoclonal antibodies to factor IX: Characterization and use in immunoassays for factor IX. Thromb. Res. 33, 211-224, 1984.
    • (1984) Thromb. Res. , vol.33 , pp. 211-224
    • Smith, K.J.1    Ono, K.2
  • 19
    • 0023109376 scopus 로고
    • Factor IX metal ion-dependent antigen assays for measurement of warfarin effect
    • SMITH, K.J., SINGARAJU, C. and SMITH, L.F. Factor IX metal ion-dependent antigen assays for measurement of warfarin effect. Am. J. Clin. Pathol. 87, 370-376, 1987.
    • (1987) Am. J. Clin. Pathol. , vol.87 , pp. 370-376
    • Smith, K.J.1    Singaraju, C.2    Smith, L.F.3
  • 21
    • 0017710978 scopus 로고
    • Characteristics of a human cell line transformed by DNA from human adenovirus type 5
    • GRAHAM, F.L., SMILEY, J., RUSSELL, W.C. and NAIRN, R. Characteristics of a human cell line transformed by DNA from human adenovirus type 5. J. Gen. Virol. 36, 59-72, 1977.
    • (1977) J. Gen. Virol. , vol.36 , pp. 59-72
    • Graham, F.L.1    Smiley, J.2    Russell, W.C.3    Nairn, R.4
  • 22
    • 0024344169 scopus 로고
    • Efficient oligonucleotide-directed construction of mutations in expression vectors by the gapped duplex DNA method using alternating selectable markers
    • STANSSENS, P., OPSOMER, C., McKEOWN, Y.M., KRAMER, W., ZABEAU, M. and FRITZ, H.J. Efficient oligonucleotide-directed construction of mutations in expression vectors by the gapped duplex DNA method using alternating selectable markers. Nucl. Acids Res. 17, 4441-4454, 1989.
    • (1989) Nucl. Acids Res. , vol.17 , pp. 4441-4454
    • Stanssens, P.1    Opsomer, C.2    McKeown, Y.M.3    Kramer, W.4    Zabeau, M.5    Fritz, H.J.6
  • 23
    • 0024394549 scopus 로고
    • Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme
    • ANDERSSON, S., DAVIS, D.L., DAHLBÄCK, H., JÖRNVALL, H. and RUSSEL, D.W. Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme. J. Biol. Chem. 264, 8222-8229,1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8222-8229
    • Andersson, S.1    Davis, D.L.2    Dahlbäck, H.3    Jörnvall, H.4    Russel, D.W.5
  • 26
    • 0023733887 scopus 로고
    • Amino-terminal alanine functions in a calcium-specific process essential for membrane binding by prothrombin fragment 1
    • WELSCH, D.J. and NELSESTUEN, G.J. Amino-terminal alanine functions in a calcium-specific process essential for membrane binding by prothrombin fragment 1. Biochemistry 27, 4939-4945, 1988.
    • (1988) Biochemistry , vol.27 , pp. 4939-4945
    • Welsch, D.J.1    Nelsestuen, G.J.2
  • 27
    • 0022450813 scopus 로고
    • Molecular basis of hemophilia B: A defective enzyme due to an unprocessed propeptide is caused by a point mutation in the factor IX precursor
    • DIUGUID, D.L., RABIET, M.J., FURIE, B.C., LIEBMAN, H.A. and FURIE, B. Molecular basis of hemophilia B: A defective enzyme due to an unprocessed propeptide is caused by a point mutation in the factor IX precursor. Proc. Natl. Acad. Sci. USA 83, 5803-5807, 1986.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5803-5807
    • Diuguid, D.L.1    Rabiet, M.J.2    Furie, B.C.3    Liebman, H.A.4    Furie, B.5
  • 28
    • 0028029621 scopus 로고
    • Profactor IX: The propeptide inhibits binding to membrane surfaces and activation by factor XIa
    • BRISTOL, J.A., FREEDMAN, S.J., FURIE, B.C. and FURIE, B. Profactor IX: The propeptide inhibits binding to membrane surfaces and activation by factor XIa. Biochemistry 33, 14136-14143, 1994.
    • (1994) Biochemistry , vol.33 , pp. 14136-14143
    • Bristol, J.A.1    Freedman, S.J.2    Furie, B.C.3    Furie, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.