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Volumn 7, Issue 3, 1998, Pages 782-788

The N-terminal segment of antithrombin acts as a steric gate for the bining of heparin

Author keywords

Antithrombin; Heparin; Kinetic analysis; N terminal segment; Thermolysin

Indexed keywords

ANTITHROMBIN; HEPARIN; THERMOLYSIN;

EID: 0031912076     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070328     Document Type: Article
Times cited : (12)

References (20)
  • 1
    • 0025269894 scopus 로고
    • Anti-thrombin Rouen-IV (24 Arg→Cys). The amino-terminal contribution to heparin binding
    • Borg JY, Brennan SO, Carrell RW, George P, Perry DJ, Shaw J. 1990. Anti-thrombin Rouen-IV (24 Arg→Cys). The amino-terminal contribution to heparin binding. FEBS Lett 266:163-166.
    • (1990) FEBS Lett , vol.266 , pp. 163-166
    • Borg, J.Y.1    Brennan, S.O.2    Carrell, R.W.3    George, P.4    Perry, D.J.5    Shaw, J.6
  • 2
    • 0001860654 scopus 로고
    • Serpins: Antithrombin and other inhibitors of coagulation and fibrinolysis: Evidence from amino acid sequences
    • Verstraete M, Vermylen J, Lijnen HR, Arnout J, eds. Leuven: Leuven University Press
    • Carrell RW, Christey PB, Boswell DR. 1987. Serpins: Antithrombin and other inhibitors of coagulation and fibrinolysis: Evidence from amino acid sequences. In: Verstraete M, Vermylen J, Lijnen HR, Arnout J, eds. Thrombosis and haemostasis. Leuven: Leuven University Press. pp 1-15.
    • (1987) Thrombosis and Haemostasis , pp. 1-15
    • Carrell, R.W.1    Christey, P.B.2    Boswell, D.R.3
  • 3
    • 0028773279 scopus 로고
    • Biological implications of a 3 Å structure of dimeric antithrombin
    • Carrell RW, Stein PE, Fermi G, Wardell MR. 1994. Biological implications of a 3 Å structure of dimeric antithrombin. Structure 2:257-270.
    • (1994) Structure , vol.2 , pp. 257-270
    • Carrell, R.W.1    Stein, P.E.2    Fermi, G.3    Wardell, M.R.4
  • 4
    • 0022622201 scopus 로고
    • Antithrombin III Basel. Identification of a Pro-Leu substitution in a hereditary abnormal antithrombin with impaired heparin cofactor activity
    • Chang JY, Tran TH. 1986. Antithrombin III Basel. Identification of a Pro-Leu substitution in a hereditary abnormal antithrombin with impaired heparin cofactor activity. J Biol Chem 261:1174-1176.
    • (1986) J Biol Chem , vol.261 , pp. 1174-1176
    • Chang, J.Y.1    Tran, T.H.2
  • 5
    • 0029866947 scopus 로고    scopus 로고
    • Probing serpin reactive-loop conformations by proteolytic cleavage
    • Chang WS, Wardell MR, Lomas DA, Carrell RW. 1996. Probing serpin reactive-loop conformations by proteolytic cleavage. Biochem J 314:647-653.
    • (1996) Biochem J , vol.314 , pp. 647-653
    • Chang, W.S.1    Wardell, M.R.2    Lomas, D.A.3    Carrell, R.W.4
  • 6
    • 0021061174 scopus 로고
    • Structure-activity relationship in heparin: A synthetic pentasaccharide with high affinity for antithrombin III and eliciting high anti-factor Xa activity
    • Choay J, Petitou M, Lormeau JC, Sinay P, Casu B, Gatti G. 1983. Structure-activity relationship in heparin: A synthetic pentasaccharide with high affinity for antithrombin III and eliciting high anti-factor Xa activity. Biochem Biophys Res Commun 116:492-499.
    • (1983) Biochem Biophys Res Commun , vol.116 , pp. 492-499
    • Choay, J.1    Petitou, M.2    Lormeau, J.C.3    Sinay, P.4    Casu, B.5    Gatti, G.6
  • 10
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of proteins
    • Kraulis P. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of proteins. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 11
    • 0018076716 scopus 로고
    • The molecular-weight-dependence of the anti-coagulant activity of heparin
    • Laurent TC, Tengblad A, Thunberg L, Höök M, Lindahl U. 1978. The molecular-weight-dependence of the anti-coagulant activity of heparin. Biochem J 175:691-701.
    • (1978) Biochem J , vol.175 , pp. 691-701
    • Laurent, T.C.1    Tengblad, A.2    Thunberg, L.3    Höök, M.4    Lindahl, U.5
  • 12
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electro-blotted onto polyvinylidene difluoride membranes
    • Matsudaira P. 1987. Sequence from picomole quantities of proteins electro-blotted onto polyvinylidene difluoride membranes. J Biol Chem 262:10035-10038.
    • (1987) J Biol Chem , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 13
    • 0019472086 scopus 로고
    • A simple two-step procedure for the isolation of antithrombin III from biological fluids
    • McKay EJ. 1981. A simple two-step procedure for the isolation of antithrombin III from biological fluids. Thromb Res 21:375-382.
    • (1981) Thromb Res , vol.21 , pp. 375-382
    • McKay, E.J.1
  • 14
    • 0001410715 scopus 로고
    • Regulation of thrombin by antithrombin and heparin cofactor II
    • Berliner LJ, ed. New York: Plenum Press
    • Olson ST, Björk I. 1992. Regulation of thrombin by antithrombin and heparin cofactor II. In: Berliner LJ, ed. Thrombin: Structure and function. New York: Plenum Press. pp 159-217.
    • (1992) Thrombin: Structure and Function , pp. 159-217
    • Olson, S.T.1    Björk, I.2
  • 15
    • 0026690347 scopus 로고
    • Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement
    • Olson ST, Björk I, Sheffer R, Craig PA, Shore JD, Choay J. 1992. Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement. J Biol Chem 267:12528-12538.
    • (1992) J Biol Chem , vol.267 , pp. 12528-12538
    • Olson, S.T.1    Björk, I.2    Sheffer, R.3    Craig, P.A.4    Shore, J.D.5    Choay, J.6
  • 16
    • 0027498670 scopus 로고
    • Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin
    • Olson ST, Björk I, Shore JD. 1993. Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin. Methods Enzymol 222:525-559.
    • (1993) Methods Enzymol , vol.222 , pp. 525-559
    • Olson, S.T.1    Björk, I.2    Shore, J.D.3
  • 17
    • 0019821957 scopus 로고
    • Binding of high affinity heparin to antithrombin III. Stopped flow kinetic studies of the binding interaction
    • Olson ST, Srinivasan KR, Björk I, Shore JD. 1981. Binding of high affinity heparin to antithrombin III. Stopped flow kinetic studies of the binding interaction. J Biol Chem 256:11073-11079.
    • (1981) J Biol Chem , vol.256 , pp. 11073-11079
    • Olson, S.T.1    Srinivasan, K.R.2    Björk, I.3    Shore, J.D.4
  • 19
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulphate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Shagger H, von Jagow G. 1987. Tricine-sodium dodecyl sulphate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166:368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Shagger, H.1    Von Jagow, G.2
  • 20
    • 0031588685 scopus 로고    scopus 로고
    • The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site
    • Skinner R, Abrahams JP, Whisstock JC, Lesk AM, Carrell RW, Wardell MR. 1997. The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site. J Mol Biol 266:601-609.
    • (1997) J Mol Biol , vol.266 , pp. 601-609
    • Skinner, R.1    Abrahams, J.P.2    Whisstock, J.C.3    Lesk, A.M.4    Carrell, R.W.5    Wardell, M.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.