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Volumn 6, Issue 2, 2001, Pages 117-127

High-level expression and characterization of single chain urokinase-type plasminogen activator (scu-PA) produced in recombinant Chinese hamster ovary (CHO) cells

Author keywords

CHO cells; Copy number; Gene amplification; MTX; pro UK; Scu PA

Indexed keywords


EID: 33748487012     PISSN: 12268372     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02931957     Document Type: Article
Times cited : (5)

References (67)
  • 1
    • 0022632219 scopus 로고
    • Urokinase-related proteins in human urine. Isolation and characterization of single-chain urokinase (prouroki-nase) and urokinase-inhibitor complex
    • Stump, D. C., M. Thienpont, and D. Collen (1986) Urokinase-related proteins in human urine. Isolation and characterization of single-chain urokinase (prouroki-nase) and urokinase-inhibitor complex. J. Biol. Chem. 261: 1267-1273.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1267-1273
    • Stump, D.C.1    Thienpont, M.2    Collen, D.3
  • 2
    • 0022387786 scopus 로고
    • Proteolytic cleavage of single-chain pro-urokinase induces conformational change which follows activation of the zymogen and reduction of its high affinity for fibrin
    • Kasai, S., H. Arimura, M. Nishida, and T. Suyama (1985) Proteolytic cleavage of single-chain pro-urokinase induces conformational change which follows activation of the zymogen and reduction of its high affinity for fibrin. J. Biol. Chem. 260: 12377-12381.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12377-12381
    • Kasai, S.1    Arimura, H.2    Nishida, M.3    Suyama, T.4
  • 3
    • 0027940373 scopus 로고
    • New recombinant glycosylated prourokinase for treatment of patients with acute myocardial infarction
    • Prourokinase Study Group
    • Weaver, W. D., J. R. Hartmann, J. L. Anderson, P. S. Reddy, J. C. Sobolski, and A. A. Sasahara (1994) New recombinant glycosylated prourokinase for treatment of patients with acute myocardial infarction. Prourokinase Study Group. J. Am. Coll. Cardiol. 24: 1242-1248.
    • (1994) J. Am. Coll. Cardiol. , vol.24 , pp. 1242-1248
    • Weaver, W.D.1    Hartmann, J.R.2    Anderson, J.L.3    Reddy, P.S.4    Sobolski, J.C.5    Sasahara, A.A.6
  • 5
    • 0020490792 scopus 로고
    • A proenzyme form of human urokinase
    • Wun, T. C., L. Ossowski, and E. Reich (1982) A proenzyme form of human urokinase. J. Biol. Chem. 257: 7262-7268.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7262-7268
    • Wun, T.C.1    Ossowski, L.2    Reich, E.3
  • 6
    • 0020198526 scopus 로고
    • The primary structure of high molecular mass urokinase from human urine. The complete amino acid sequence of the A chain
    • Gunzler, W. A., G. J. Steffens, F. Otting, S. M. Kim, E. Frankus, and L. Flohe (1982) The primary structure of high molecular mass urokinase from human urine. The complete amino acid sequence of the A chain. Hoppe-Seyler's Z. Physiol. Chem. 363: 1155-1165.
    • (1982) Hoppe-Seyler's Z. Physiol. Chem. , vol.363 , pp. 1155-1165
    • Gunzler, W.A.1    Steffens, G.J.2    Otting, F.3    Kim, S.M.4    Frankus, E.5    Flohe, L.6
  • 7
    • 0026737620 scopus 로고
    • Domain structure and interactions of recombinant urokinase-type plasminogen activator
    • Novokhatny V., L. Medved, A. Mazar, P. Marcotte, J. Henkin, and K. Ingham (1992) Domain structure and interactions of recombinant urokinase-type plasminogen activator. J. Biol. Chem. 267: 3878-3885.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3878-3885
    • Novokhatny, V.1    Medved, L.2    Mazar, A.3    Marcotte, P.4    Henkin, J.5    Ingham, K.6
  • 8
    • 0020664546 scopus 로고
    • Purification and partial characterization of a single-chain high-molecular-weight form of urokinase from human urine
    • Husain, S. S., V. Gurewich, and B. Lipinski (1983) Purification and partial characterization of a single-chain high-molecular-weight form of urokinase from human urine. Arch. Biochem. Biophys. 220: 31-38.
    • (1983) Arch. Biochem. Biophys. , vol.220 , pp. 31-38
    • Husain, S.S.1    Gurewich, V.2    Lipinski, B.3
  • 9
    • 0023022473 scopus 로고
    • The activation of pro-urokinase by plasma kallikrein and its inactivation by thrombin
    • Ichinose, A., K. Fujikawa, and T Suyama (1986) The activation of pro-urokinase by plasma kallikrein and its inactivation by thrombin. J. Biol. Chem. 261: 3486-3489.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3486-3489
    • Ichinose, A.1    Fujikawa, K.2    Suyama, T.3
  • 10
    • 0025845425 scopus 로고
    • Cathepsin B efficiently activates the soluble and the tumor cell receptor-bound form of the proenzyme urokinase-type plasminogen activator (Pro-uPA)
    • Kobayashi, H, M. Schmitt, L. Goretzki, N. Chucholowski, J. Calvete, M. Kramer, W. A. Gunzler, F. Janicke, and H. Graeff (1991) Cathepsin B efficiently activates the soluble and the tumor cell receptor-bound form of the proenzyme urokinase-type plasminogen activator (Pro-uPA). J. Biol. Chem. 266: 5147-5152.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5147-5152
    • Kobayashi, H.1    Schmitt, M.2    Goretzki, L.3    Chucholowski, N.4    Calvete, J.5    Kramer, M.6    Gunzler, W.A.7    Janicke, F.8    Graeff, H.9
  • 11
    • 0028211344 scopus 로고
    • Platelet-bound prekallikrein promotes pro-urokinase-induced clot lysis: A mechanism for targeting the factor XII dependent intrinsic pathway of fibrinolysis
    • Loza, J. P., V. Gurewich, M. Johnstone, and R. Pannell (1994) Platelet-bound prekallikrein promotes pro-urokinase-induced clot lysis: a mechanism for targeting the factor XII dependent intrinsic pathway of fibrinolysis. Thromb. Haemost. 71: 347-352.
    • (1994) Thromb. Haemost. , vol.71 , pp. 347-352
    • Loza, J.P.1    Gurewich, V.2    Johnstone, M.3    Pannell, R.4
  • 12
    • 0021260107 scopus 로고
    • Effective and fibrin-specific clot lysis by a zymogen precursor form of urokinase (prourokinase). A study in vitro and in two animal species
    • Gurewich, V., R. Pannell, S. Louie, P. Kelley R. L. Suddith, and R. Greenlee (1984) Effective and fibrin-specific clot lysis by a zymogen precursor form of urokinase (prourokinase). A study in vitro and in two animal species. J. Clin. Invest. 73: 1731-1739.
    • (1984) J. Clin. Invest. , vol.73 , pp. 1731-1739
    • Gurewich, V.1    Pannell, R.2    Louie, S.3    Kelley, P.4    Suddith, R.L.5    Greenlee, R.6
  • 13
    • 0021172255 scopus 로고
    • Biological and thrombolytic properties of proenzyme and active forms of human urokinase: I. Fibrinolytic and fibrinogenolytic properties in human plasma in vitro of urokinases obtained from human urine or by recombinant DNA technology
    • Zamarron, C., H. R. Lijnen, B. Van Hoef, and D. Collen (1984) Biological and thrombolytic properties of proenzyme and active forms of human urokinase: I. Fibrinolytic and fibrinogenolytic properties in human plasma in vitro of urokinases obtained from human urine or by recombinant DNA technology. Thromb. Haemost. 52: 19-23.
    • (1984) Thromb. Haemost. , vol.52 , pp. 19-23
    • Zamarron, C.1    Lijnen, H.R.2    Van Hoef, B.3    Collen, D.4
  • 14
    • 0026776671 scopus 로고
    • Fragment E-2 from fibrin substantially enhances pro-urokinase-induced Glu-plasminogen activation. A kinetic study using the plasmin-resistant mutant pro-urokinase Ala-158-rpro-UK
    • Liu, J. N. and V. Gurewich (1992) Fragment E-2 from fibrin substantially enhances pro-urokinase-induced Glu-plasminogen activation. A kinetic study using the plasmin-resistant mutant pro-urokinase Ala-158-rpro-UK. Biochemistry 31: 6311-6317.
    • (1992) Biochemistry , vol.31 , pp. 6311-6317
    • Liu, J.N.1    Gurewich, V.2
  • 15
    • 0021144347 scopus 로고
    • Biological and thrombolytic properties of proenzyme and active forms of human urokinase: III. Thrombolytic properties of natural and recombinant urokinase in rabbits with experimental jugular vein thrombosis
    • Collen, D., J. M. Stassen, M. Blaber, M. Winkler, and M. Verstraete (1984) Biological and thrombolytic properties of proenzyme and active forms of human urokinase: III. Thrombolytic properties of natural and recombinant urokinase in rabbits with experimental jugular vein thrombosis. Thromb. Haemost. 52: 27-30.
    • (1984) Thromb. Haemost. , vol.52 , pp. 27-30
    • Collen, D.1    Stassen, J.M.2    Blaber, M.3    Winkler, M.4    Verstraete, M.5
  • 16
    • 0023266773 scopus 로고
    • Thrombolysis with recombinant human single-chain urokinase-type plasminogen activator (rscu-PA): Dose-response in dogs with coronary artery thrombosis
    • Van de Werf, F., I. K. Jang, and D. Collen (1987) Thrombolysis with recombinant human single-chain urokinase-type plasminogen activator (rscu-PA): dose-response in dogs with coronary artery thrombosis. J. Cardiovasc. Pharmacol. 9: 91-93.
    • (1987) J. Cardiovasc. Pharmacol. , vol.9 , pp. 91-93
    • Van De Werf, F.1    Jang, I.K.2    Collen, D.3
  • 17
    • 0028930385 scopus 로고
    • Low incidence of hemorrhagic infarction following coronary reperfusion with nasaruplase in a canine model of acute myocardial infarction. Comparison with recombinant t-PA
    • Kido, H., K. Hayashi, T. Uchida, and M. Watanabe (1995) Low incidence of hemorrhagic infarction following coronary reperfusion with nasaruplase in a canine model of acute myocardial infarction. Comparison with recombinant t-PA. Jpn. Heart J. 36: 61-79.
    • (1995) Jpn. Heart J. , vol.36 , pp. 61-79
    • Kido, H.1    Hayashi, K.2    Uchida, T.3    Watanabe, M.4
  • 18
    • 0013224738 scopus 로고    scopus 로고
    • Recombinant glycosylated pro-urokinase: Biochemistry, pharmacology, and early clinical experience
    • Sasahara, A. A., and J. Loscalzo (eds.). Marcel Dekker, NY, USA
    • Credo, R. B., J. C. Sobolski, W. D. Weaver, and J. R. Hartmann (1997) Recombinant glycosylated pro-urokinase: biochemistry, pharmacology, and early clinical experience. pp. 561-589. In: Sasahara, A. A., and J. Loscalzo (eds.). New Therapeutic Agents in Thrombosis and Thromobolysis. Marcel Dekker, NY, USA.
    • (1997) New Therapeutic Agents in Thrombosis and Thromobolysis , pp. 561-589
    • Credo, R.B.1    Sobolski, J.C.2    Weaver, W.D.3    Hartmann, J.R.4
  • 19
    • 0027419518 scopus 로고
    • Pro-urokinase and prekallikrein are both associated with platelets. Implications for the intrinsic pathway of fibrinolysis and for therapeutic thrombolysis
    • Gurewich, V., M. Johnstone, J. P. Loza, and R. Pannell (1993) Pro-urokinase and prekallikrein are both associated with platelets. Implications for the intrinsic pathway of fibrinolysis and for therapeutic thrombolysis. FEBS Lett. 318: 317-321.
    • (1993) FEBS Lett. , vol.318 , pp. 317-321
    • Gurewich, V.1    Johnstone, M.2    Loza, J.P.3    Pannell, R.4
  • 20
    • 0020064684 scopus 로고
    • Isolation and characterization of urokinase from human plasma
    • Wun, T. C., W. D. Schleuning, and E. Reich (1982) Isolation and characterization of urokinase from human plasma. J. Biol. Chem. 257: 3276-3283.
    • (1982) J. Biol. Chem. , vol.257 , pp. 3276-3283
    • Wun, T.C.1    Schleuning, W.D.2    Reich, E.3
  • 21
    • 0020352040 scopus 로고
    • Purification of zymogen to plasminogen activator from human glioblastoma cells by affinity chromatography with monoclonal antibody
    • Nielsen, L. S., J. G. Hansen, L. Skriver, E. L. Wilson, K. Kaltoft, J. Zeuthen, and K. Dano (1982) Purification of zymogen to plasminogen activator from human glioblastoma cells by affinity chromatography with monoclonal antibody. Biochemistry 21: 6410-6415.
    • (1982) Biochemistry , vol.21 , pp. 6410-6415
    • Nielsen, L.S.1    Hansen, J.G.2    Skriver, L.3    Wilson, E.L.4    Kaltoft, K.5    Zeuthen, J.6    Dano, K.7
  • 22
    • 0029969280 scopus 로고    scopus 로고
    • Characterization of single chain urokinase-type plasminogen activator with a novel amino-acid substitution in the kringle structure
    • Yoshimoto, M., Y. Ushiyama, M. Sakai, S. Tamaki, H. Hara, K. Takahashi, Y. Sawasaki, and K. Hanada (1996) Characterization of single chain urokinase-type plasminogen activator with a novel amino-acid substitution in the kringle structure. Biochim. Biophys. Acta. 1293: 83-89.
    • (1996) Biochim. Biophys. Acta , vol.1293 , pp. 83-89
    • Yoshimoto, M.1    Ushiyama, Y.2    Sakai, M.3    Tamaki, S.4    Hara, H.5    Takahashi, K.6    Sawasaki, Y.7    Hanada, K.8
  • 23
    • 0022360938 scopus 로고
    • Primary structure of single-chain pro-urokinase
    • Kasai, S., H. Arimura, M. Nishida, and T. Suyama (1985) Primary structure of single-chain pro-urokinase. J. Biol. Chem. 260: 12382-12389.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12382-12389
    • Kasai, S.1    Arimura, H.2    Nishida, M.3    Suyama, T.4
  • 27
    • 0025142701 scopus 로고
    • Evolutionary assembly of blood coagulation proteins
    • Patthy L. (1990) Evolutionary assembly of blood coagulation proteins. Semin. Thromb. Hemost. 16: 245-259.
    • (1990) Semin. Thromb. Hemost. , vol.16 , pp. 245-259
    • Patthy, L.1
  • 28
    • 0026528796 scopus 로고
    • High expression vectors for the production of recombinant single-chain urinary plasminogen activator from Escherichia coli
    • Brigelius-Flohe, R., G. Steffens, W. Strassburger, and L. Flohe (1992) High expression vectors for the production of recombinant single-chain urinary plasminogen activator from Escherichia coli. Appl. Microbiol. Biotechnol. 36: 640-649.
    • (1992) Appl. Microbiol. Biotechnol. , vol.36 , pp. 640-649
    • Brigelius-Flohe, R.1    Steffens, G.2    Strassburger, W.3    Flohe, L.4
  • 30
    • 0023664285 scopus 로고
    • Characterization of recombinant human single chain urokinase-type plasminogen activator mutants produced by site-specific mutagenesis of lysine 158
    • Nelles, L., H. R. Lijnen, D. Collen, and W. E. Holmes (1987) Characterization of recombinant human single chain urokinase-type plasminogen activator mutants produced by site-specific mutagenesis of lysine 158. J. Biol. Chem. 262: 5682-5689.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5682-5689
    • Nelles, L.1    Lijnen, H.R.2    Collen, D.3    Holmes, W.E.4
  • 31
    • 11944254486 scopus 로고
    • Spin filter perfusion system for high density cell culture: Production of recombinant urinary type plasminogen activator in CHO cells
    • Avgerinos, G. C., D. Drapeau, J. S. Socolow, J. I. Mao, K. Hsiao, and R. J. Broeze (1990) Spin filter perfusion system for high density cell culture: production of recombinant urinary type plasminogen activator in CHO cells. Bio/Technol. 8: 54-58.
    • (1990) Bio/Technol. , vol.8 , pp. 54-58
    • Avgerinos, G.C.1    Drapeau, D.2    Socolow, J.S.3    Mao, J.I.4    Hsiao, K.5    Broeze, R.J.6
  • 32
    • 0027134293 scopus 로고
    • Stable production of recombinant pro-urokinase by human lymphoblastoid Namalwa KJM-1 cells: Host-cell dependency of the expressed-protein stability
    • Satoh, M., S. Hosoi, H. Miyaji, S. Itoh, and S. Sato (1993) Stable production of recombinant pro-urokinase by human lymphoblastoid Namalwa KJM-1 cells: host-cell dependency of the expressed-protein stability. Cytotechnology 13: 79-88.
    • (1993) Cytotechnology , vol.13 , pp. 79-88
    • Satoh, M.1    Hosoi, S.2    Miyaji, H.3    Itoh, S.4    Sato, S.5
  • 33
    • 0028961625 scopus 로고
    • Production of recombinant proteins in Chinese hamster ovary cells using a protein-free cell culture medium
    • Zang, M., H. Trautmann, C. Gandor, F. Messi, F. Asselbergs, C. Leist, A. Fiechter, and J. Reiser (1995) Production of recombinant proteins in Chinese hamster ovary cells using a protein-free cell culture medium. Bio/Tech-nol. 13: 389-392.
    • (1995) Bio/Technol. , vol.13 , pp. 389-392
    • Zang, M.1    Trautmann, H.2    Gandor, C.3    Messi, F.4    Asselbergs, F.5    Leist, C.6    Fiechter, A.7    Reiser, J.8
  • 34
    • 0020367363 scopus 로고
    • Transmural, haemorrhagic myocardial infarction after intracoronary streptokinase. Clinical, angiographic, and necropsy findings
    • Mathey D. G., J. Schofer, K. H. Kuck, U. Beil, and G. Kloppel (1982) Transmural, haemorrhagic myocardial infarction after intracoronary streptokinase. Clinical, angiographic, and necropsy findings. Br. Heart J. 48: 546-551.
    • (1982) Br. Heart J. , vol.48 , pp. 546-551
    • Mathey, D.G.1    Schofer, J.2    Kuck, K.H.3    Beil, U.4    Kloppel, G.5
  • 35
    • 0024686628 scopus 로고
    • Tissue-type plasminogen activator mutants. Theoretical and clinical considerations
    • Bang, N. U. (1989) Tissue-type plasminogen activator mutants. Theoretical and clinical considerations. Circulation 79: 1391-1392.
    • (1989) Circulation , vol.79 , pp. 1391-1392
    • Bang, N.U.1
  • 36
    • 0030723376 scopus 로고    scopus 로고
    • Thrombolytic therapy of acute myocardial infarction with saruplase, a single-chain urokinase-type plasminogen activator (scu-PA) from recombinant bacteria
    • Tebbe, U., W. A. Gunzler, G. R. Hopkins, T. Grymbowski, and H. Barth (1997) Thrombolytic therapy of acute myocardial infarction with saruplase, a single-chain urokinase-type plasminogen activator (scu-PA) from recombinant bacteria. Fibrinol. Proteolysis 11: 45-54.
    • (1997) Fibrinol. Proteolysis , vol.11 , pp. 45-54
    • Tebbe, U.1    Gunzler, W.A.2    Hopkins, G.R.3    Grymbowski, T.4    Barth, H.5
  • 37
    • 0021834045 scopus 로고
    • Coronary thrombolysis in dogs with intravenously administered human prourokinase
    • Collen, D., D. Stump, F. van de Werf, I. K. Jang, M. Nobuhara, and H. R. Lijnen (1985) Coronary thrombolysis in dogs with intravenously administered human prourokinase. Circulation 72: 384-388.
    • (1985) Circulation , vol.72 , pp. 384-388
    • Collen, D.1    Stump, D.2    Van De Werf, F.3    Jang, I.K.4    Nobuhara, M.5    Lijnen, H.R.6
  • 38
    • 0001127374 scopus 로고
    • Isolation of Chinese hamster cell mutants deficient in dihydrofolate reductase activity
    • Urlaub, G. and L. A. Chasin (1980) Isolation of Chinese hamster cell mutants deficient in dihydrofolate reductase activity. Proc. Natl. Acad. Sci. USA 77: 4216-4220.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 4216-4220
    • Urlaub, G.1    Chasin, L.A.2
  • 39
    • 0020400592 scopus 로고
    • Amplification and expression of sequences cotransfected with a modular dihydrofolate reductase complementary DNA gene
    • Kaufman, R. J. and P. A. Sharp (1982) Amplification and expression of sequences cotransfected with a modular dihydrofolate reductase complementary DNA gene. J. Mol. Biol. 159: 601-621.
    • (1982) J. Mol. Biol. , vol.159 , pp. 601-621
    • Kaufman, R.J.1    Sharp, P.A.2
  • 40
    • 0022100495 scopus 로고
    • Coamplification and coexpression of human tissue-type plasminogen activator and murine dihydrofolate reductase sequences in Chinese hamster ovary cells
    • Kaufman, R. J., L. C. Wasley A. J. Spiliotes, S. D. Gossels, S. A. Latt, G. R. Larsen, and R. M. Kay (1985) Coamplification and coexpression of human tissue-type plasminogen activator and murine dihydrofolate reductase sequences in Chinese hamster ovary cells. Mol. Cell. Biol. 5: 1750-1759.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 1750-1759
    • Kaufman, R.J.1    Wasley, L.C.2    Spiliotes, A.J.3    Gossels, S.D.4    Latt, S.A.5    Larsen, G.R.6    Kay, R.M.7
  • 41
    • 0020540147 scopus 로고
    • Role of carbohydrate in multimeric structure of factor VHI/von Willebrand factor protein
    • Gralnick, H. R., S. B. Williams, and M. E. Rick (1983) Role of carbohydrate in multimeric structure of factor VHI/von Willebrand factor protein. Proc. Natl. Acad. Sci. USA 80: 2771-2774.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2771-2774
    • Gralnick, H.R.1    Williams, S.B.2    Rick, M.E.3
  • 43
    • 0025365149 scopus 로고
    • Selection and coamplification of heterologous genes in mammalian cells
    • Kaufman, R. J. (1990) Selection and coamplification of heterologous genes in mammalian cells. Methods Enzymol. 185: 537-566.
    • (1990) Methods Enzymol. , vol.185 , pp. 537-566
    • Kaufman, R.J.1
  • 44
    • 14744277083 scopus 로고
    • High level expression of the humanized monoclonal antibody Campath-1H in Chinese hamster ovary cells
    • Page, M. J. and M. A. Sydenham (1991) High level expression of the humanized monoclonal antibody Campath-1H in Chinese hamster ovary cells. Bio/Technol. 9: 64-68.
    • (1991) Bio/Technol. , vol.9 , pp. 64-68
    • Page, M.J.1    Sydenham, M.A.2
  • 45
    • 52549097989 scopus 로고    scopus 로고
    • Development of high density mammalian cell culture system for the production of tissue-type plasminogen
    • Park, B. G., J. M. Chun, G. T. Lee, I. H. Kim, and Y. H. Jeong (2000) Development of high density mammalian cell culture system for the production of tissue-type plasminogen. Biotechnol. Bioprocess Eng. 5: 123-129.
    • (2000) Biotechnol. Bioprocess Eng. , vol.5 , pp. 123-129
    • Park, B.G.1    Chun, J.M.2    Lee, G.T.3    Kim, I.H.4    Jeong, Y.H.5
  • 46
    • 0019813877 scopus 로고
    • Amplification and loss of dihydrofolate reductase genes in a Chinese hamster ovary cell line
    • Kaufman, R. J. and R. T. Schimke (1981) Amplification and loss of dihydrofolate reductase genes in a Chinese hamster ovary cell line. Mol. Cell. Biol. 1: 1069-1076.
    • (1981) Mol. Cell. Biol. , vol.1 , pp. 1069-1076
    • Kaufman, R.J.1    Schimke, R.T.2
  • 47
    • 0024411328 scopus 로고
    • Recent progress in understanding mechanisms of mammalian DNA amplification
    • Stark, G. R., M. Debatisse, E. Giulotto, and G. M. Wahl (1989) Recent progress in understanding mechanisms of mammalian DNA amplification. Cell 57: 901-908.
    • (1989) Cell , vol.57 , pp. 901-908
    • Stark, G.R.1    Debatisse, M.2    Giulotto, E.3    Wahl, G.M.4
  • 48
    • 0002598959 scopus 로고    scopus 로고
    • Characterization of chimeric antibody producing CHO cells in the course of dihydrofolate reductase-mediated gene amplification and their stability in the absence of selective pressure
    • Kim, S. J., N. S. Kim, C. J. Ryu, H. J. Hong, and G. M. Lee (1998) Characterization of chimeric antibody producing CHO cells in the course of dihydrofolate reductase-mediated gene amplification and their stability in the absence of selective pressure. Biotechnol. Bioeng. 58: 73-84.
    • (1998) Biotechnol. Bioeng. , vol.58 , pp. 73-84
    • Kim, S.J.1    Kim, N.S.2    Ryu, C.J.3    Hong, H.J.4    Lee, G.M.5
  • 49
    • 0020574233 scopus 로고
    • Deletion of the diploid dihydrofolate reductase locus from cultured mammalian cells
    • Urlaub, G., E. Kas, A. M. Carothers, and L. A. Chasin (1983) Deletion of the diploid dihydrofolate reductase locus from cultured mammalian cells. Cell 33: 405-412.
    • (1983) Cell , vol.33 , pp. 405-412
    • Urlaub, G.1    Kas, E.2    Carothers, A.M.3    Chasin, L.A.4
  • 50
    • 0029198092 scopus 로고
    • The optimization of serum-free medium for the production of the scu-PA by the addition of algal extracts
    • Kim, H. G., K. D. Sung, M. S. Ham, K. H. Chung, K. H. Chung, and H. Y. Lee (1995) The optimization of serum-free medium for the production of the scu-PA by the addition of algal extracts. Cytotechnology 17: 165-172.
    • (1995) Cytotechnology , vol.17 , pp. 165-172
    • Kim, H.G.1    Sung, K.D.2    Ham, M.S.3    Chung, K.H.4    Chung, K.H.5    Lee, H.Y.6
  • 51
    • 85047678943 scopus 로고    scopus 로고
    • Performance study of perfusion cultures for the production of single-chain urokinase-type plasminogen activator (scu-PA) in a 2.5 L spin-filter bioreactor
    • Jo, E. C., J. W. Yun, S. I. Jung, K. H. Chung, and J. H. Kim (1998) Performance study of perfusion cultures for the production of single-chain urokinase-type plasminogen activator (scu-PA) in a 2.5 L spin-filter bioreactor. Bioproc. Eng. 19: 363-372.
    • (1998) Bioproc. Eng. , vol.19 , pp. 363-372
    • Jo, E.C.1    Yun, J.W.2    Jung, S.I.3    Chung, K.H.4    Kim, J.H.5
  • 52
    • 0023405059 scopus 로고
    • Polyadenylation of Chinese hamster dihydrofolate reductase genomic genes and minigenes after gene transfer
    • Venolia, L., G. Urlaub, and L. A. Chasin (1987) Polyadenylation of Chinese hamster dihydrofolate reductase genomic genes and minigenes after gene transfer. Somat. Cell. Mol. Genet. 13: 491-504.
    • (1987) Somat. Cell. Mol. Genet. , vol.13 , pp. 491-504
    • Venolia, L.1    Urlaub, G.2    Chasin, L.A.3
  • 53
    • 0021356824 scopus 로고
    • Phenotypic expression in Escherichia coli and nucleotide sequence of two Chinese hamster lung cell cDNAs encoding different dihydrofolate reductases
    • Melera, P. W., J. P. Davide, C. A. Hession, and K. W. Scotto (1984) Phenotypic expression in Escherichia coli and nucleotide sequence of two Chinese hamster lung cell cDNAs encoding different dihydrofolate reductases. Mol. Cell. Biol. 4: 38-48.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 38-48
    • Melera, P.W.1    Davide, J.P.2    Hession, C.A.3    Scotto, K.W.4
  • 54
    • 0022623039 scopus 로고
    • Multiple transcription start sites, DNase I-hypersensitive sites, and an opposite-strand exon in the 5′ region of the CHO dhfr gene
    • Mitchell, P. J., A. M. Carothers, J. H. Han, J. D. Harding, E. Kas, L. Venolia, and L. A. Chasin (1986) Multiple transcription start sites, DNase I-hypersensitive sites, and an opposite-strand exon in the 5′ region of the CHO dhfr gene. Mol. Cell. Biol. 6: 425-440.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 425-440
    • Mitchell, P.J.1    Carothers, A.M.2    Han, J.H.3    Harding, J.D.4    Kas, E.5    Venolia, L.6    Chasin, L.A.7
  • 56
    • 52549085004 scopus 로고    scopus 로고
    • Immobilization of rat kidney glomerular mesangial cell and its coculture with glomerular epitherial cell
    • Kida, T., S. Fujishima, M. Matsumura, and P. C. Wang (2000) Immobilization of rat kidney glomerular mesangial cell and its coculture with glomerular epitherial cell. Biotechnol. Bioprocess Eng. 5: 92-98.
    • (2000) Biotechnol. Bioprocess Eng. , vol.5 , pp. 92-98
    • Kida, T.1    Fujishima, S.2    Matsumura, M.3    Wang, P.C.4
  • 57
    • 0018799065 scopus 로고
    • Studies on the fibrinolytic system in human plasma: Quantitative determination of plasminogen activators and proactivators
    • Kluft, C. (1979) Studies on the fibrinolytic system in human plasma: quantitative determination of plasminogen activators and proactivators. Thromb. Haemost. 41: 365-383.
    • (1979) Thromb. Haemost. , vol.41 , pp. 365-383
    • Kluft, C.1
  • 58
    • 0022965391 scopus 로고
    • Differential detection of single-chain and two-chain urokinase-type plasminogen activator by a new immunoadsorbent-amidolytic assay (IAA)
    • Corti, A., M. L. Nolli, and G. Cassani (1986) Differential detection of single-chain and two-chain urokinase-type plasminogen activator by a new immunoadsorbent-amidolytic assay (IAA). Thromb. Haemost. 56: 407-410.
    • (1986) Thromb. Haemost. , vol.56 , pp. 407-410
    • Corti, A.1    Nolli, M.L.2    Cassani, G.3
  • 59
    • 0025844947 scopus 로고
    • Analysis of genes and chromosomes by nonisotopic in situ hybridization
    • Lichter, P., A. L. Boyle, T. Cremer, and D. C. Ward (1991) Analysis of genes and chromosomes by nonisotopic in situ hybridization. Genet. Anal. Tech. Appl. 8: 24-35.
    • (1991) Genet. Anal. Tech. Appl. , vol.8 , pp. 24-35
    • Lichter, P.1    Boyle, A.L.2    Cremer, T.3    Ward, D.C.4
  • 60
    • 0025678648 scopus 로고
    • Chinese hamster ovary cells continuously secrete a cysteine endopeptidase
    • Satoh, M., S. Hosoi, and S. Sato (1990) Chinese hamster ovary cells continuously secrete a cysteine endopeptidase. In Vitro Cell. Dev. Biol. 26: 1101-1104.
    • (1990) In Vitro Cell. Dev. Biol. , vol.26 , pp. 1101-1104
    • Satoh, M.1    Hosoi, S.2    Sato, S.3
  • 61
    • 0023918719 scopus 로고
    • Synthesis, processing, and secretion of recombinant human factor VIII expressed in mammalian cells
    • Kaufman, R. J., L. C. Wasley and A. J. Dorner (1988) Synthesis, processing, and secretion of recombinant human factor VIII expressed in mammalian cells. J. Biol. Chem. 263: 6352-6362.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6352-6362
    • Kaufman, R.J.1    Wasley, L.C.2    Dorner, A.J.3
  • 62
    • 0025083117 scopus 로고
    • Carbohydrate composition and presence of a fucoseprotein linkage in recombinant human pro-urokinase
    • Kentzer, E. J., A. Buko, G. Menon, and V. K. Sarin (1990) Carbohydrate composition and presence of a fucoseprotein linkage in recombinant human pro-urokinase. Biochem. Biophys. Res. Commun. 171: 401-406.
    • (1990) Biochem. Biophys. Res. Commun. , vol.171 , pp. 401-406
    • Kentzer, E.J.1    Buko, A.2    Menon, G.3    Sarin, V.K.4
  • 63
    • 0026451175 scopus 로고
    • The influence of glycosylation on the catalytic and fibrinolytic properties of pro-urokinase
    • Lenich, C., R. Pannell, J. Henkin, and V. Gurewich (1992) The influence of glycosylation on the catalytic and fibrinolytic properties of pro-urokinase. Thromb. Haemost. 68: 539-544.
    • (1992) Thromb. Haemost. , vol.68 , pp. 539-544
    • Lenich, C.1    Pannell, R.2    Henkin, J.3    Gurewich, V.4
  • 64
    • 0024948946 scopus 로고
    • A nuclear DNA attachment element mediates elevated and position-independent gene activity
    • Stief, A., D. M. Winter, W. H. Stratling, and A. E. Sippel (1989) A nuclear DNA attachment element mediates elevated and position-independent gene activity. Nature 341: 343-345.
    • (1989) Nature , vol.341 , pp. 343-345
    • Stief, A.1    Winter, D.M.2    Stratling, W.H.3    Sippel, A.E.4
  • 65
    • 0025869479 scopus 로고
    • Scaffold-attached regions from the human interferon beta domain can be used to enhance the stable expression of genes under the control of various promoters
    • Klehr, D., K. Maass, and J. Bode (1991) Scaffold-attached regions from the human interferon beta domain can be used to enhance the stable expression of genes under the control of various promoters. Biochemistry 30: 1264-1270.
    • (1991) Biochemistry , vol.30 , pp. 1264-1270
    • Klehr, D.1    Maass, K.2    Bode, J.3
  • 66
    • 0028286165 scopus 로고
    • Expansions of transgene repeats cause heterochromatin formation and gene silencing in Drosophila
    • Dorer, D. R. and S. Henikoff (1994) Expansions of transgene repeats cause heterochromatin formation and gene silencing in Drosophila. Cell 77: 993-1002.
    • (1994) Cell , vol.77 , pp. 993-1002
    • Dorer, D.R.1    Henikoff, S.2
  • 67
    • 0028988485 scopus 로고
    • Position-independent transgene expression mediated by boundary elements from the apolipoprotein B chromatin domain
    • Kalos, M. and R. E. Fournier (1995) Position-independent transgene expression mediated by boundary elements from the apolipoprotein B chromatin domain. Mol. Cell. Biol. 15: 198-207.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 198-207
    • Kalos, M.1    Fournier, R.E.2


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