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Volumn 106, Issue 2, 2002, Pages 157-164

Separation of active and inactive forms of human antithrombin by heparin affinity chromatography

Author keywords

Active and inactive isoforms; Antithrombin; Heparin affinity chromatography; Latent antithrombin

Indexed keywords

ANTITHROMBIN; HEPARIN; ISOPROTEIN; PROTEINASE;

EID: 0037089061     PISSN: 00493848     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0049-3848(02)00097-X     Document Type: Article
Times cited : (27)

References (29)
  • 1
    • 0032538299 scopus 로고    scopus 로고
    • Implications for function and therapy of a 2.9 A structure of binary-complexed antithrombin
    • Skinner R., Chang W.S., Jin L., Pei X., Huntington J.A., Abrahams J.P.et al. Implications for function and therapy of a 2.9 A structure of binary-complexed antithrombin. J. Mol. Biol. 283:1998;9-14.
    • (1998) J. Mol. Biol. , vol.283 , pp. 9-14
    • Skinner, R.1    Chang, W.S.2    Jin, L.3    Pei, X.4    Huntington, J.A.5    Abrahams, J.P.6
  • 4
    • 0031041451 scopus 로고    scopus 로고
    • Inhibitory mechanism of serpins. Mobility of the C-terminal region of the reactive-site loop
    • Hopkins P.C.R., Chang W.-S.W., Wardell M.R., Stone S.R. Inhibitory mechanism of serpins. Mobility of the C-terminal region of the reactive-site loop. J. Biol. Chem. 272:1997;3905-3909.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3905-3909
    • Hopkins, P.C.R.1    Chang, W.-S.W.2    Wardell, M.R.3    Stone, S.R.4
  • 5
    • 0029591826 scopus 로고
    • The inhibition mechanism of serpins, evidence that the mobile reactive center loop is cleaved in the native protease-inhibitor complex
    • Wilczynska M., Fa M., Ohlsson P.-I., Ny T. The inhibition mechanism of serpins, evidence that the mobile reactive center loop is cleaved in the native protease-inhibitor complex. J. Biol. Chem. 270:1995;29652-29655.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29652-29655
    • Wilczynska, M.1    Fa, M.2    Ohlsson, P.-I.3    Ny, T.4
  • 7
    • 0028407364 scopus 로고
    • Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop
    • Wei A., Rubin H., Cooperman B.S., Christianson D.W. Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop. Nat. Struct. Biol. 1:1994;251-258.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 251-258
    • Wei, A.1    Rubin, H.2    Cooperman, B.S.3    Christianson, D.W.4
  • 9
    • 0031059479 scopus 로고    scopus 로고
    • Commercial antithrombin concentrate contains inactive L-forms of antithrombin
    • Chang W.-S.W., Harper P.L. Commercial antithrombin concentrate contains inactive L-forms of antithrombin. Thromb. Haemost. 77:1997;323-328.
    • (1997) Thromb. Haemost. , vol.77 , pp. 323-328
    • Chang, W.-S.W.1    Harper, P.L.2
  • 10
    • 0022616168 scopus 로고
    • Pasteurisation induced changes in an antithrombin III concentrate
    • Winkelman L., Haddon M.E. Pasteurisation induced changes in an antithrombin III concentrate. Thromb. Res. 43:1986;219-227.
    • (1986) Thromb. Res. , vol.43 , pp. 219-227
    • Winkelman, L.1    Haddon, M.E.2
  • 11
    • 0019866346 scopus 로고
    • Thermal denaturation of antithrombin III: Stabilization by heparin and lyotropic anions
    • Busby T.F., Atha D.H., Ingham K.C. Thermal denaturation of antithrombin III: stabilization by heparin and lyotropic anions. J. Biol. Chem. 256:1981;12140-12147.
    • (1981) J. Biol. Chem. , vol.256 , pp. 12140-12147
    • Busby, T.F.1    Atha, D.H.2    Ingham, K.C.3
  • 12
    • 0030700799 scopus 로고    scopus 로고
    • Preparative induction and characterization of L-antithrombin: A structural homologue of latent plasminogen activator inhibitor-1
    • Wardell M.R., Chang W.-S.W., Bruce D., Skinner R., Lesk A.M., Carrell R.W. Preparative induction and characterization of L-antithrombin: a structural homologue of latent plasminogen activator inhibitor-1. Biochemistry. 36:1997;13133-13142.
    • (1997) Biochemistry , vol.36 , pp. 13133-13142
    • Wardell, M.R.1    Chang, W.-S.W.2    Bruce, D.3    Skinner, R.4    Lesk, A.M.5    Carrell, R.W.6
  • 13
    • 0033570979 scopus 로고    scopus 로고
    • Formation of the antithrombin heterodimer in vivo and the onset of thrombosis
    • Zhou A., Huntington J.A., Carrell R.W. Formation of the antithrombin heterodimer in vivo and the onset of thrombosis. Blood. 94:1999;3388-3390.
    • (1999) Blood , vol.94 , pp. 3388-3390
    • Zhou, A.1    Huntington, J.A.2    Carrell, R.W.3
  • 14
    • 0028773279 scopus 로고
    • Biological implications of a 3 A structure of dimeric antithrombin
    • Carrell R.W., Stein P.E., Fermi G., Wardell M.R. Biological implications of a 3 A structure of dimeric antithrombin. Structure. 2:1994;257-270.
    • (1994) Structure , vol.2 , pp. 257-270
    • Carrell, R.W.1    Stein, P.E.2    Fermi, G.3    Wardell, M.R.4
  • 15
    • 0000925011 scopus 로고
    • Analysis of protein concentration by gel electrophoresis
    • T.E. Creighton. Oxford, UK: IRL
    • Goldenberg D.P. Analysis of protein concentration by gel electrophoresis. Creighton T.E. Protein Structure: A Practical Approach. 1989;225-250 IRL, Oxford, UK.
    • (1989) Protein Structure: A Practical Approach , pp. 225-250
    • Goldenberg, D.P.1
  • 16
    • 0019792891 scopus 로고
    • Analysis of protein and peptide mixtures. Evaluation of three sodium dodecylsulphate-polyacrylamide gel electrophoresis buffer systems
    • Bury A.F. Analysis of protein and peptide mixtures. Evaluation of three sodium dodecylsulphate-polyacrylamide gel electrophoresis buffer systems. J. Chromatogr. 213:1981;491-500.
    • (1981) J. Chromatogr. , vol.213 , pp. 491-500
    • Bury, A.F.1
  • 17
    • 0031568263 scopus 로고    scopus 로고
    • Polyacrylamide gel electrophoresis in discontinuous transverse urea-gradient gels
    • Gentile F., Veneziani B.M., Sellitto C. Polyacrylamide gel electrophoresis in discontinuous transverse urea-gradient gels. Anal. Biochem. 244:1997;228-232.
    • (1997) Anal. Biochem. , vol.244 , pp. 228-232
    • Gentile, F.1    Veneziani, B.M.2    Sellitto, C.3
  • 18
    • 0033578910 scopus 로고    scopus 로고
    • Antiangiogenic activity of the cleaved conformation of the serpin antithrombin
    • O'Reilly M.S., Pirie-Shepherd S., Lane W.S., Folkman J. Antiangiogenic activity of the cleaved conformation of the serpin antithrombin. Science. 285:1999;1926-1928.
    • (1999) Science , vol.285 , pp. 1926-1928
    • O'Reilly, M.S.1    Pirie-Shepherd, S.2    Lane, W.S.3    Folkman, J.4
  • 19
    • 0033578657 scopus 로고    scopus 로고
    • How serpins are shaping up
    • Carrell R.W. How serpins are shaping up. Science. 285:1999;1862-1863.
    • (1999) Science , vol.285 , pp. 1862-1863
    • Carrell, R.W.1
  • 20
    • 0034544536 scopus 로고    scopus 로고
    • Antiangiogenic effects of latent antithrombin through perturbed cell-matrix interactions and apoptosis of endothelial cells
    • Larsson H., Sjöblom T., Dixelius J., Östman A., Ylinenjärvi K., Björk J.et al. Antiangiogenic effects of latent antithrombin through perturbed cell-matrix interactions and apoptosis of endothelial cells. Cancer Res. 60:2000;6723-6729.
    • (2000) Cancer Res. , vol.60 , pp. 6723-6729
    • Larsson, H.1    Sjöblom, T.2    Dixelius, J.3    Östman, A.4    Ylinenjärvi, K.5    Björk, J.6
  • 21
    • 0035853699 scopus 로고    scopus 로고
    • A novel anti-angiogenic form of antithrombin with retained proteinase binding ability and heparin affinity
    • Larsson H., Akernd P., Nordling K., Raub-Segall E., Claesson-Welsh L., Björk J. A novel anti-angiogenic form of antithrombin with retained proteinase binding ability and heparin affinity. J. Biol. Chem. 276(15):2001;11996-12002.
    • (2001) J. Biol. Chem. , vol.276 , Issue.15 , pp. 11996-12002
    • Larsson, H.1    Akernd, P.2    Nordling, K.3    Raub-Segall, E.4    Claesson-Welsh, L.5    Björk, J.6
  • 22
    • 0031570290 scopus 로고    scopus 로고
    • Effect of individual carbohydrate chains of recombinant antithrombin on heparin affinity and on the generation of glycoforms differing in heparin affinity
    • Olson S.T., Frances-Chmura A.M., Swanson R., Björk I., Zettlmeissl G. Effect of individual carbohydrate chains of recombinant antithrombin on heparin affinity and on the generation of glycoforms differing in heparin affinity. Arch. Biochem. Biophys. 341:1997;212-221.
    • (1997) Arch. Biochem. Biophys. , vol.341 , pp. 212-221
    • Olson, S.T.1    Frances-Chmura, A.M.2    Swanson, R.3    Björk, I.4    Zettlmeissl, G.5
  • 23
    • 0030917184 scopus 로고    scopus 로고
    • The oligosaccharide side chain on Asn-135 of α-antithrombin, absent in β-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change
    • Turk B., Brieditis I., Bock S.C., Olson S.T., Björk I. The oligosaccharide side chain on Asn-135 of α-antithrombin, absent in β-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change. Biochemistry. 36:1997;6682-6691.
    • (1997) Biochemistry , vol.36 , pp. 6682-6691
    • Turk, B.1    Brieditis, I.2    Bock, S.C.3    Olson, S.T.4    Björk, I.5
  • 24
    • 0023917034 scopus 로고
    • High-performance affinity chromatography of proteins on TSKgel Heparin-5PW
    • Nakamura K., Toyoda K., Kato Y. High-performance affinity chromatography of proteins on TSKgel Heparin-5PW. J. Chromatogr. 446:1988;234-238.
    • (1988) J. Chromatogr. , vol.446 , pp. 234-238
    • Nakamura, K.1    Toyoda, K.2    Kato, Y.3
  • 25
    • 0021991632 scopus 로고
    • Isolation and characterization of an antithrombin III variant with reduced carbohydrate content and enhanced heparin binding
    • Peterson C.B., Blackbura M.N. Isolation and characterization of an antithrombin III variant with reduced carbohydrate content and enhanced heparin binding. J. Biol. Chem. 260:1985;610-615.
    • (1985) J. Biol. Chem. , vol.260 , pp. 610-615
    • Peterson, C.B.1    Blackbura, M.N.2
  • 26
    • 0018191834 scopus 로고
    • Microheterogeneity of human antithrombin III
    • Borsodi A., Narasimhan T.R. Microheterogeneity of human antithrombin III. Br. J. Haematol. 39:1978;121-127.
    • (1978) Br. J. Haematol. , vol.39 , pp. 121-127
    • Borsodi, A.1    Narasimhan, T.R.2
  • 27
    • 0034064387 scopus 로고    scopus 로고
    • Salmon antithrombin has only three carbohydrate side chains, and shows functional similarities to human β-antithrombin
    • Andersen Ø., Flengsrud R., Norberg K., Salte R. Salmon antithrombin has only three carbohydrate side chains, and shows functional similarities to human β-antithrombin. Eur. J. Biochem. 267:2000;1651-1657.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1651-1657
    • Andersen, Ø.1    Flengsrud, R.2    Norberg, K.3    Salte, R.4
  • 28
    • 0021416620 scopus 로고
    • Gel electrophoresis in studies of protein conformation and folding
    • Goldenberg D.P., Creighton T.E. Gel electrophoresis in studies of protein conformation and folding. Anal. Biochem. 138:1984;1-8.
    • (1984) Anal. Biochem. , vol.138 , pp. 1-8
    • Goldenberg, D.P.1    Creighton, T.E.2
  • 29
    • 0033537843 scopus 로고    scopus 로고
    • Oxidation of methionine residues in antithrombin. Effects on biological activity and heparin binding
    • Van Patten S.M., Hanson E., Bernasconi R., Zhang K., Manavalan P., Cole E.S.et al. Oxidation of methionine residues in antithrombin. Effects on biological activity and heparin binding. J. Biol. Chem. 274(15):1999;10268-10276.
    • (1999) J. Biol. Chem. , vol.274 , Issue.15 , pp. 10268-10276
    • Van Patten, S.M.1    Hanson, E.2    Bernasconi, R.3    Zhang, K.4    Manavalan, P.5    Cole, E.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.