메뉴 건너뛰기




Volumn 68, Issue 4, 2000, Pages 407-421

Modification of a recombinant GPI-anchored metalloproteinase for secretion alters the protein glycosylation

Author keywords

CHO; Glycosylation; Leishmanolysin; Mammalian; Metalloproteinase; Recombinant protein production

Indexed keywords

AMINES; CELL MEMBRANES; ENZYME KINETICS; MASS SPECTROMETRY; METALLORGANIC POLYMERS; PHYSIOLOGICAL MODELS; PHYSIOLOGY; PROTEINS;

EID: 0034690650     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(20000520)68:4<407::AID-BIT6>3.0.CO;2-S     Document Type: Article
Times cited : (3)

References (73)
  • 1
    • 0028061380 scopus 로고
    • The effect of cell-culture conditions on the oligosaccharide structures of secreted glycoproteins
    • Andersen D. Goochee CF. 1994. The effect of cell-culture conditions on the oligosaccharide structures of secreted glycoproteins. Curr Opin Biotechnol 5:546-549.
    • (1994) Curr Opin Biotechnol , vol.5 , pp. 546-549
    • Andersen, D.1    Goochee, C.F.2
  • 2
    • 0342558323 scopus 로고
    • Carbohydrate specific receptors of the liver
    • Ashwell G, Hartford J. 1992. Carbohydrate specific receptors of the liver. Annu Rev Biochem 51:5.11-554.
    • (1992) Annu Rev Biochem , vol.51 , pp. 511-554
    • Ashwell, G.1    Hartford, J.2
  • 3
    • 0027471552 scopus 로고
    • Primary structure of N-linked carbohydrate chains of a human chimeric plasminogen activator K2tu-PA expressed in Chinese hamster ovary cells
    • Bergwerff AA, van Oostrum J, Asselbergs FAM, Burgi R, Hokke C, Kamerling JP, Vliegenthart FG. 1993. Primary structure of N-linked carbohydrate chains of a human chimeric plasminogen activator K2tu-PA expressed in Chinese hamster ovary cells. Eur J Biochem 212: 639-656.
    • (1993) Eur J Biochem , vol.212 , pp. 639-656
    • Bergwerff, A.A.1    Van Oostrum, J.2    Asselbergs, F.A.M.3    Burgi, R.4    Hokke, C.5    Kamerling, J.P.6    Vliegenthart, F.G.7
  • 4
    • 0030051045 scopus 로고    scopus 로고
    • Cell line and site specific comparative analysis of the N-linked oligosaccharides on human ICAM-1des454-532 by electrospray ionization mass spectrometry
    • Bloom JW, Madanat MS, Kay MS. 1996. Cell line and site specific comparative analysis of the N-linked oligosaccharides on human ICAM-1des454-532 by electrospray ionization mass spectrometry. Biochemistry 35:1856-1864.
    • (1996) Biochemistry , vol.35 , pp. 1856-1864
    • Bloom, J.W.1    Madanat, M.S.2    Kay, M.S.3
  • 5
    • 14744285958 scopus 로고
    • Culture pH affects expression rates and glycosylation of recombinant mouse placental lactogen proteins in Chinese hamster ovary (CHO) cells
    • Borys MC, Linzer DI, Papoutsakis ET. 1993. Culture pH affects expression rates and glycosylation of recombinant mouse placental lactogen proteins in Chinese hamster ovary (CHO) cells. Bio/Technology 11: 720-724.
    • (1993) Bio/Technology , vol.11 , pp. 720-724
    • Borys, M.C.1    Linzer, D.I.2    Papoutsakis, E.T.3
  • 6
    • 0029046678 scopus 로고
    • Role of the Leishmania surface protease GP63 in complement fixation, cell adhesion, and resistance to complement-mediated lysis
    • Brittingham A, Morrison CJ, McMaster WR, McGwire B, Chang KP, Mosser DM. 1995. Role of the Leishmania surface protease GP63 in complement fixation, cell adhesion, and resistance to complement-mediated lysis. J Immunol 155:3102-3111.
    • (1995) J Immunol , vol.155 , pp. 3102-3111
    • Brittingham, A.1    Morrison, C.J.2    McMaster, W.R.3    McGwire, B.4    Chang, K.P.5    Mosser, D.M.6
  • 7
    • 0023837354 scopus 로고
    • Molecular cloning of the major surface antigen of Leishmania
    • Button LL, McMaster WR. 1988. Molecular cloning of the major surface antigen of Leishmania. J Exp Med 167:724-729.
    • (1988) J Exp Med , vol.167 , pp. 724-729
    • Button, L.L.1    McMaster, W.R.2
  • 8
    • 0027428114 scopus 로고
    • Recombinant Leishmania surface glycoprotein GP63 is secreted in the baculovirus expression system as a latent metalloproteinase
    • Button LL, Wilson G, Astell CR, McMaster WR. 1993. Recombinant Leishmania surface glycoprotein GP63 is secreted in the baculovirus expression system as a latent metalloproteinase. Gene 134:75-81.
    • (1993) Gene , vol.134 , pp. 75-81
    • Button, L.L.1    Wilson, G.2    Astell, C.R.3    McMaster, W.R.4
  • 9
    • 0029154039 scopus 로고
    • Rapid turnover and impaired cell-surface expression of the human folate receptor in mouse L(tk-) fibroblasts, a cell line defective in glycosylphosphatidylinositol tail synthesis
    • Chung K, Roberts S, Kim CH, Kirassova M, Trepel J, Elwood PC. 1995. Rapid turnover and impaired cell-surface expression of the human folate receptor in mouse L(tk-) fibroblasts, a cell line defective in glycosylphosphatidylinositol tail synthesis. Arch Biochem Biophys 322:228-234.
    • (1995) Arch Biochem Biophys , vol.322 , pp. 228-234
    • Chung, K.1    Roberts, S.2    Kim, C.H.3    Kirassova, M.4    Trepel, J.5    Elwood, P.C.6
  • 10
    • 0027141144 scopus 로고
    • Effective immunization against cutaneous leishmaniasis with recombinant bacille Calmette-Guerin expressing the Leishmania surface proteinase GP63
    • Connell ND, Medina-Acosta H, McMaster WR, Bloom BR, Russell DG. 1993. Effective immunization against cutaneous leishmaniasis with recombinant bacille Calmette-Guerin expressing the Leishmania surface proteinase GP63. Proc Natl Acad Sci USA 90:11473-11477.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11473-11477
    • Connell, N.D.1    Medina-Acosta, H.2    McMaster, W.R.3    Bloom, B.R.4    Russell, D.G.5
  • 11
    • 0025981417 scopus 로고
    • Glycosylation of recombinant protein therapeutics: Control and functional implications
    • Cumming DA. 1991. Glycosylation of recombinant protein therapeutics: control and functional implications. Glycobiology 1:115-130.
    • (1991) Glycobiology , vol.1 , pp. 115-130
    • Cumming, D.A.1
  • 13
    • 0028885690 scopus 로고
    • Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities
    • Dell A, Morris HR, Easton R, Panico M, Patankar M, Oehninger S, Koistinen R, Seppala M, Clark GF. 1995. Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities. J Biol Chem 270:24116-241126.
    • (1995) J Biol Chem , vol.270 , pp. 24116-241126
    • Dell, A.1    Morris, H.R.2    Easton, R.3    Panico, M.4    Patankar, M.5    Oehninger, S.6    Koistinen, R.7    Seppala, M.8    Clark, G.F.9
  • 14
    • 0023038374 scopus 로고
    • The major surface protein of Leishmania promastigotes is a protease
    • Etges R, Bouvier J, Bordier C. 1986. The major surface protein of Leishmania promastigotes is a protease. J Biol Chem 261:9098-9101.
    • (1986) J Biol Chem , vol.261 , pp. 9098-9101
    • Etges, R.1    Bouvier, J.2    Bordier, C.3
  • 15
    • 0032488276 scopus 로고    scopus 로고
    • Chinese hamster ovary cells with constitutively expressed sialidase anti-sense RNA produce recombinant DNase in batch culture with increased sialic acid
    • Ferrari J, Gunson J, Lofgren J, Krumen L, Warner T. 1998. Chinese hamster ovary cells with constitutively expressed sialidase anti-sense RNA produce recombinant DNase in batch culture with increased sialic acid. Biotechnol Bioeng 60:589-595.
    • (1998) Biotechnol Bioeng , vol.60 , pp. 589-595
    • Ferrari, J.1    Gunson, J.2    Lofgren, J.3    Krumen, L.4    Warner, T.5
  • 16
    • 0029636508 scopus 로고
    • Fluorophore-labeled carbohydrate analysis of immunoglobulin fusion proteins: Correlation of oligosaccharide content with in vivo clearance profile
    • Flesher AR, Marzowski J, Wang W, Raff HV. 1994. Fluorophore-labeled carbohydrate analysis of immunoglobulin fusion proteins: Correlation of oligosaccharide content with in vivo clearance profile. Biotechnol Bioeng 46:399-407.
    • (1994) Biotechnol Bioeng , vol.46 , pp. 399-407
    • Flesher, A.R.1    Marzowski, J.2    Wang, W.3    Raff, H.V.4
  • 17
    • 0022256777 scopus 로고
    • The structure of branched lactosaminoglycans with novel disialosyl (sialyl α2-9 sialyl) terminals isolated from PA1 human embryonal carcinoma cells
    • Fukuda M, Dell A, Oates JE, Fukuda M. 1985. The structure of branched lactosaminoglycans with novel disialosyl (sialyl α2-9 sialyl) terminals isolated from PA1 human embryonal carcinoma cells. J Biol Chem 260:6623-6631.
    • (1985) J Biol Chem , vol.260 , pp. 6623-6631
    • Fukuda, M.1    Dell, A.2    Oates, J.E.3    Fukuda, M.4
  • 18
    • 0023895599 scopus 로고
    • A membrane-anchored form but not secretory form of the human chorionic gonadotropin α chain acquires polylactosaminoglycan
    • Fukuda M, Guan J, Rose JK. 1988. A membrane-anchored form but not secretory form of the human chorionic gonadotropin α chain acquires polylactosaminoglycan. J Biol Chem 263:5314-5318.
    • (1988) J Biol Chem , vol.263 , pp. 5314-5318
    • Fukuda, M.1    Guan, J.2    Rose, J.K.3
  • 19
    • 0032485239 scopus 로고    scopus 로고
    • Ammonium ion and glucosamine dependent increases in oligosaccharide complexity in recombinant glycoproteins secreted from cultivated BHK-21 cells
    • Gawlitzek M, Valley U, Wagner R. 1998. Ammonium ion and glucosamine dependent increases in oligosaccharide complexity in recombinant glycoproteins secreted from cultivated BHK-21 cells. Biotechnol Bioeng 57:518-528.
    • (1998) Biotechnol Bioeng , vol.57 , pp. 518-528
    • Gawlitzek, M.1    Valley, U.2    Wagner, R.3
  • 20
    • 0030219388 scopus 로고    scopus 로고
    • Why mammalian cell surface proteins are glycoproteins
    • Gahmberg C, Tolvanen M. 1996. Why mammalian cell surface proteins are glycoproteins. Trends Biol Sci 21:308-311.
    • (1996) Trends Biol Sci , vol.21 , pp. 308-311
    • Gahmberg, C.1    Tolvanen, M.2
  • 21
    • 0032488375 scopus 로고    scopus 로고
    • Monitoring recombinant interferon-γ N-glycosylation during perfused fluidized-bed and stirred-tank batch culture of CHO cells
    • Goldman MH, James DC, Rendall M, Ison A, Hoare M, Bull AT. 1998. Monitoring recombinant interferon-γ N-glycosylation during perfused fluidized-bed and stirred-tank batch culture of CHO cells. Biotechnol Bioeng 60:596-607.
    • (1998) Biotechnol Bioeng , vol.60 , pp. 596-607
    • Goldman, M.H.1    James, D.C.2    Rendall, M.3    Ison, A.4    Hoare, M.5    Bull, A.T.6
  • 22
    • 0027628305 scopus 로고
    • Glycosidase activity in Chinese hamster ovary cell lysate and cell culture supernatant
    • Gramer MJ, Goochee CF. 1993. Glycosidase activity in Chinese hamster ovary cell lysate and cell culture supernatant. Biotechnol Prog 9: 366-373.
    • (1993) Biotechnol Prog , vol.9 , pp. 366-373
    • Gramer, M.J.1    Goochee, C.F.2
  • 23
    • 0029053768 scopus 로고
    • Removal of sialic acid from a glycoprotein in CHO cell culture supernatant by action of an extracellular CHO cell sialidase
    • Gramer MJ, Goochee CF, Chook VY, Brousseau DT, Sliwkowski MA. 1995. Removal of sialic acid from a glycoprotein in CHO cell culture supernatant by action of an extracellular CHO cell sialidase. Bio/ Technology 13:692-698.
    • (1995) Bio/ Technology , vol.13 , pp. 692-698
    • Gramer, M.J.1    Goochee, C.F.2    Chook, V.Y.3    Brousseau, D.T.4    Sliwkowski, M.A.5
  • 24
    • 0028172722 scopus 로고
    • Purification and characterization of α-L-fucosidase from chinese hamster ovary cell culture supernatant
    • Gramer MJ, Schaffer DV, Sliwkowski MA, Goochee CF. 1994. Purification and characterization of α-L-fucosidase from Chinese hamster ovary cell culture supernatant. Glycobiology 4:611-616.
    • (1994) Glycobiology , vol.4 , pp. 611-616
    • Gramer, M.J.1    Schaffer, D.V.2    Sliwkowski, M.A.3    Goochee, C.F.4
  • 25
    • 0343417086 scopus 로고    scopus 로고
    • Site-and branch-specific sialylation of recombinant human interferon-γ in Chinese hamster ovary cell culture
    • Gu X, Harmon BJ, Wang DIC. 1997a. Site-and branch-specific sialylation of recombinant human interferon-γ in Chinese hamster ovary cell culture. Biotechnol Bioeng 55:390-398.
    • (1997) Biotechnol Bioeng , vol.55 , pp. 390-398
    • Gu, X.1    Harmon, B.J.2    Wang, D.I.C.3
  • 26
    • 0343417035 scopus 로고    scopus 로고
    • Influence of primatone RL supplementation on sialylation of recombinant human interferon-γ produced by Chinese hamster ovary cell culture using serum free media
    • Gu X, Xie L, Harmon BJ, Wang DIC. 1997b. Influence of primatone RL supplementation on sialylation of recombinant human interferon-γ produced by Chinese hamster ovary cell culture using serum free media. Biotechnol Bioeng 56:353-360.
    • (1997) Biotechnol Bioeng , vol.56 , pp. 353-360
    • Gu, X.1    Xie, L.2    Harmon, B.J.3    Wang, D.I.C.4
  • 27
    • 0032551285 scopus 로고    scopus 로고
    • Improvement of interferon-γ sialylation in Chinese hamster ovary cell culture by feeding of N-acetylmannosamine
    • Gu X, Wang DIC. 1998. Improvement of interferon-γ sialylation in Chinese hamster ovary cell culture by feeding of N-acetylmannosamine. Biotechnol Bioeng 58:642-648.
    • (1998) Biotechnol Bioeng , vol.58 , pp. 642-648
    • Gu, X.1    Wang, D.I.C.2
  • 28
    • 0023935092 scopus 로고
    • Cell-surface expression of a membrane-anchored form of the human chorionic gonadotropin-α subunit
    • Guan J, Cao H, Rose JK. 1988. Cell-surface expression of a membrane-anchored form of the human chorionic gonadotropin-α subunit. J Biol Chem 263:5306-5313.
    • (1988) J Biol Chem , vol.263 , pp. 5306-5313
    • Guan, J.1    Cao, H.2    Rose, J.K.3
  • 29
    • 0023790733 scopus 로고
    • Functional effects of asparagine-linked oligosaccharide on natural and variant human tissue type plasminogen activator
    • Hansen L, Blue Y, Barone K, Collen D, Larsen DR. 1988. Functional effects of asparagine-linked oligosaccharide on natural and variant human tissue type plasminogen activator. J Biol Chem 263: 15713-15719.
    • (1988) J Biol Chem , vol.263 , pp. 15713-15719
    • Hansen, L.1    Blue, Y.2    Barone, K.3    Collen, D.4    Larsen, D.R.5
  • 30
    • 0026733430 scopus 로고
    • Comparative study of the sugar chains of factor VIII purified from human plasma and from the culture media of recombinant baby hamster kidney cells
    • Hironaka T, Furukawa K, Esmon PC, Fournel MA, Sawada S, Kato M, Minaga T, Kobata A. 1992. Comparative study of the sugar chains of factor VIII purified from human plasma and from the culture media of recombinant baby hamster kidney cells. J Biol Chem 267:8012-8020.
    • (1992) J Biol Chem , vol.267 , pp. 8012-8020
    • Hironaka, T.1    Furukawa, K.2    Esmon, P.C.3    Fournel, M.A.4    Sawada, S.5    Kato, M.6    Minaga, T.7    Kobata, A.8
  • 32
    • 0031979830 scopus 로고    scopus 로고
    • The glycosylation heterogeneity of recombinant human IFN-γ
    • Hooker A, James D. 1998. The glycosylation heterogeneity of recombinant human IFN-γ. J Interferon Cytokine Res 18:287-295.
    • (1998) J Interferon Cytokine Res , vol.18 , pp. 287-295
    • Hooker, A.1    James, D.2
  • 33
    • 0028296148 scopus 로고
    • Expression of an enzymatically active glycosylphosphatidylinositol-anchored form of neutral endopeptidase (EC 3.4.24.11) in COS cells
    • Howell S, Lanctot C, Boileau G, Crine P. 1994. Expression of an enzymatically active glycosylphosphatidylinositol-anchored form of neutral endopeptidase (EC 3.4.24.11) in COS cells. Biochem J 299: 171-176.
    • (1994) Biochem J , vol.299 , pp. 171-176
    • Howell, S.1    Lanctot, C.2    Boileau, G.3    Crine, P.4
  • 34
    • 0032030416 scopus 로고    scopus 로고
    • Human keratinocyte growth factor recombinantly expressed in Chinese hamster ovary cells: Isolation of isoforms and characterization of post-translational modifications
    • Hsu YR, Hsu WJ, Viswanatham K, Brankow B, Tseng J, Hu S, Morris CF, Kenney WC, Hsieng SL. 1998. Human keratinocyte growth factor recombinantly expressed in Chinese hamster ovary cells: Isolation of isoforms and characterization of post-translational modifications. Prot Expression Purif 12:189-200.
    • (1998) Prot Expression Purif , vol.12 , pp. 189-200
    • Hsu, Y.R.1    Hsu, W.J.2    Viswanatham, K.3    Brankow, B.4    Tseng, J.5    Hu, S.6    Morris, C.F.7    Kenney, W.C.8    Hsieng, S.L.9
  • 35
    • 0027368961 scopus 로고
    • Recombinant soluble human FcγRII: Production, characterization and inhibition of the arthus reaction
    • Ierino FL, Powell MS, McKenzie IFC, Hogarth PM. 1993. Recombinant soluble human FcγRII: Production, characterization and inhibition of the arthus reaction. J Exp Med 178:1617-1628.
    • (1993) J Exp Med , vol.178 , pp. 1617-1628
    • Ierino, F.L.1    Powell, M.S.2    McKenzie, I.F.C.3    Hogarth, P.M.4
  • 37
    • 0028224656 scopus 로고
    • Glycosylation of recombinant proteins: Problems and prospects
    • Jenkins N, Curling MA. 1994. Glycosylation of recombinant proteins: Problems and prospects. Enzyme Microb Technol 16:354-364.
    • (1994) Enzyme Microb Technol , vol.16 , pp. 354-364
    • Jenkins, N.1    Curling, M.A.2
  • 38
    • 0028910204 scopus 로고
    • Monitoring and control of recombinant glycoprotein heterogeneity in animal cell cultures
    • Jenkins N. 1995. Monitoring and control of recombinant glycoprotein heterogeneity in animal cell cultures. Biochem Soc Trans 23:171-175.
    • (1995) Biochem Soc Trans , vol.23 , pp. 171-175
    • Jenkins, N.1
  • 39
    • 0029837484 scopus 로고    scopus 로고
    • Getting the glycosylation right: Implications for the biotechnology industry
    • Jenkins N, Parekh RB, James DC. 1996. Getting the glycosylation right: Implications for the biotechnology industry. Nat Biotechnol 14: 975-981.
    • (1996) Nat Biotechnol , vol.14 , pp. 975-981
    • Jenkins, N.1    Parekh, R.B.2    James, D.C.3
  • 40
    • 0024207853 scopus 로고
    • Comparative study of the asparagine-linked sugar chains of natural human interteron-β1 and recombinant interferon-β1 produced by three different mammalian cells
    • Kawaga Y, Takasaki S, Utsumi J, Hosoi K, Shimizu H, Kochibe N, Kobata A. 1988. Comparative study of the asparagine-linked sugar chains of natural human interteron-β1 and recombinant interferon-β1 produced by three different mammalian cells. J Biol Chem 263:17508-17515.
    • (1988) J Biol Chem , vol.263 , pp. 17508-17515
    • Kawaga, Y.1    Takasaki, S.2    Utsumi, J.3    Hosoi, K.4    Shimizu, H.5    Kochibe, N.6    Kobata, A.7
  • 41
    • 0029731590 scopus 로고    scopus 로고
    • The sialoadhesions - A family of sialic acid - Dependent cellular recognition molecules within the immunoglobulin superfamily
    • Kelm S, Schauer R, Crocker PR. 1996. The sialoadhesions - a family of sialic acid - dependent cellular recognition molecules within the immunoglobulin superfamily. Glycoconjugate J 13:916-926.
    • (1996) Glycoconjugate J , vol.13 , pp. 916-926
    • Kelm, S.1    Schauer, R.2    Crocker, P.R.3
  • 42
    • 0027909728 scopus 로고
    • Controlled release process to recover heterologous glycosylphosphatidylinositol membrane anchored proteins from CHO cells
    • Kennard ML, Food MR, Jefferies WA, Piret JM. 1993. Controlled release process to recover heterologous glycosylphosphatidylinositol membrane anchored proteins from CHO cells. Biotechnol Bioeng 42: 480-486.
    • (1993) Biotechnol Bioeng , vol.42 , pp. 480-486
    • Kennard, M.L.1    Food, M.R.2    Jefferies, W.A.3    Piret, J.M.4
  • 43
    • 0342992506 scopus 로고
    • Glycosylation of CD4: Expression in Chinese hamster ovary cells and partial characterization of the oligosaccharides
    • Konig R, Ashwell G, Hanover JA. 1989. Glycosylation of CD4: Expression in Chinese hamster ovary cells and partial characterization of the oligosaccharides. Membr Technol 64:89-106.
    • (1989) Membr Technol , vol.64 , pp. 89-106
    • Konig, R.1    Ashwell, G.2    Hanover, J.A.3
  • 44
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld R, Kornfeld S. 1985. Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 54:631-664.
    • (1985) Annu Rev Biochem , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 45
    • 0027582384 scopus 로고
    • Oligosaccharide reprocessing and recycling of a cell surface glycoprotein in cultured rat hepatocyles
    • Kreisel W, Hildebrandt H, Mossner W, Tauber R, Reutter W. 1992. Oligosaccharide reprocessing and recycling of a cell surface glycoprotein in cultured rat hepatocyles. Biol Chem Hoppe-Seyler 374:255-263.
    • (1992) Biol Chem Hoppe-Seyler , vol.374 , pp. 255-263
    • Kreisel, W.1    Hildebrandt, H.2    Mossner, W.3    Tauber, R.4    Reutter, W.5
  • 46
    • 0024321508 scopus 로고
    • Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of β-galactosidase α-2,6-sialytransferase
    • Lee E, Roth J, Paulson JC. 1989. Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of β-galactosidase α-2,6-sialytransferase. J Biol Chem 264:13848-13855.
    • (1989) J Biol Chem , vol.264 , pp. 13848-13855
    • Lee, E.1    Roth, J.2    Paulson, J.C.3
  • 47
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type I recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • Leonard CK, Spellman MW, Riddle L, Harris RJ, Thomas JN, Gregory TJ. 1990. Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type I recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J Biol Chem 265:10373-10382.
    • (1990) J Biol Chem , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5    Gregory, T.J.6
  • 48
    • 0018844844 scopus 로고
    • Structure of an unusual complex type oligosaccharide isolated from Chinese hamster ovary cells
    • Li E, Gibson R, Kornfeld S. 1980. Structure of an unusual complex type oligosaccharide isolated from Chinese hamster ovary cells. Arch Biochem Biophys 199:393-399.
    • (1980) Arch Biochem Biophys , vol.199 , pp. 393-399
    • Li, E.1    Gibson, R.2    Kornfeld, S.3
  • 50
    • 0000291882 scopus 로고
    • Covalently attached phosphatidylinositol as a Hydrophobic anchor for membrane proteins
    • Low MG, Ferguson MAJ, Futerman AH, Silman I. 1986. Covalently attached phosphatidylinositol as a Hydrophobic anchor for membrane proteins. Trends Biochem Sci 11:212-215.
    • (1986) Trends Biochem Sci , vol.11 , pp. 212-215
    • Low, M.G.1    Ferguson, M.A.J.2    Futerman, A.H.3    Silman, I.4
  • 51
    • 0028972393 scopus 로고
    • Analysis of the active site and activation mechanism of the Leishmania surface metal loproteinase GP63
    • Macdonald MH, Morrison CJ, McMaster WR. 1995. Analysis of the active site and activation mechanism of the Leishmania surface metal loproteinase GP63. Biochim Biophys Acta 1253:199-207.
    • (1995) Biochim Biophys Acta , vol.1253 , pp. 199-207
    • Macdonald, M.H.1    Morrison, C.J.2    McMaster, W.R.3
  • 52
    • 0029294124 scopus 로고
    • Tissue plasminogen activator co-expressed in Chinese hamster ovary cells with α-(2,6)-sialyltransferase contains NeuAcα(2,6)Galβ(1,4)Glc-N-AcR linkages
    • Minch SL, Kallio PT, Bailey JE. 1995. Tissue plasminogen activator co-expressed in Chinese hamster ovary cells with α-(2,6)-sialyltransferase contains NeuAcα(2,6)Galβ(1,4)Glc-N-AcR linkages. Biotechnol Prog 11:348-351.
    • (1995) Biotechnol Prog , vol.11 , pp. 348-351
    • Minch, S.L.1    Kallio, P.T.2    Bailey, J.E.3
  • 53
    • 0027256304 scopus 로고
    • Differential effect of various inhibitors on four types of rat sialidase
    • Miyagi T, Hata K, Hasegawa A, Aoyagi T. 1993. Differential effect of various inhibitors on four types of rat sialidase. Glycocongujate J 10:45-49.
    • (1993) Glycocongujate J , vol.10 , pp. 45-49
    • Miyagi, T.1    Hata, K.2    Hasegawa, A.3    Aoyagi, T.4
  • 54
    • 1842301079 scopus 로고    scopus 로고
    • Differential stability of proteolytically active and inactive recombinant metalloproteinase in Chinese hamster ovary cells
    • Morrison CJ, McMaster WR, Piret JM. 1997. Differential stability of proteolytically active and inactive recombinant metalloproteinase in Chinese hamster ovary cells. Biotechnol Bioeng 53:594-600.
    • (1997) Biotechnol Bioeng , vol.53 , pp. 594-600
    • Morrison, C.J.1    McMaster, W.R.2    Piret, J.M.3
  • 55
    • 0030198722 scopus 로고    scopus 로고
    • Sialidase activity in culture fluid of Chinese hamster ovary cells during batch culture and its effect on recombinant human antithrombin III integrity
    • Munzert E, Muthing J, Buntemeyer H, Lehman J. 1996. Sialidase activity in culture fluid of Chinese hamster ovary cells during batch culture and its effect on recombinant human antithrombin III integrity. Biotechnol Prog 12:559-563.
    • (1996) Biotechnol Prog , vol.12 , pp. 559-563
    • Munzert, E.1    Muthing, J.2    Buntemeyer, H.3    Lehman, J.4
  • 56
    • 0028105757 scopus 로고
    • Polypeptide and carbohydrate structure of recombinant human interleukin-6 produced in Chinese hamster ovary cells
    • Orita T, Oh-eda M, Hasegawa M, Kuboniwa H, Esaki K, Ochi N. 1994. Polypeptide and carbohydrate structure of recombinant human interleukin-6 produced in Chinese hamster ovary cells. J Biochem 115: 345-350.
    • (1994) J Biochem , vol.115 , pp. 345-350
    • Orita, T.1    Oh-eda, M.2    Hasegawa, M.3    Kuboniwa, H.4    Esaki, K.5    Ochi, N.6
  • 58
    • 0024415963 scopus 로고
    • N-Glycosylation and in vitro enzymatic activity of human recombinant tissue plasminogen activator expressed in Chinese hamster ovary cells
    • Parekh RB, Dwek RA, Rudd PM, Thomas JR, Rademacher TW, Wun TC, Herbert B, Reitz B, Palmier M. 1989. N-Glycosylation and in vitro enzymatic activity of human recombinant tissue plasminogen activator expressed in Chinese hamster ovary cells. Biochemistry 28:7670-7679.
    • (1989) Biochemistry , vol.28 , pp. 7670-7679
    • Parekh, R.B.1    Dwek, R.A.2    Rudd, P.M.3    Thomas, J.R.4    Rademacher, T.W.5    Wun, T.C.6    Herbert, B.7    Reitz, B.8    Palmier, M.9
  • 59
    • 0024355330 scopus 로고
    • Glycoproteins: What are the sugar chains for?
    • Paulson JC. 1989. Glycoproteins: What are the sugar chains for? Trends Biol Sci 14:272-276.
    • (1989) Trends Biol Sci , vol.14 , pp. 272-276
    • Paulson, J.C.1
  • 60
    • 0025055605 scopus 로고
    • Transfection of human α-(1-3)fucosyltransferase gene into Chinese hamster ovary cells
    • Potvin B, Kumar R, Howard DR, Stanley P. 1990. Transfection of human α-(1-3)fucosyltransferase gene into Chinese hamster ovary cells. J Biol Chem 265:1615-1622.
    • (1990) J Biol Chem , vol.265 , pp. 1615-1622
    • Potvin, B.1    Kumar, R.2    Howard, D.R.3    Stanley, P.4
  • 61
    • 0032552221 scopus 로고    scopus 로고
    • Anti-sense strategies for glycosylation engineering of Chinese hamster ovary (CHO) cells
    • Prati EGP, Scheidegger P, Sburiati AR, Bailey JE. 1998. Anti-sense strategies for glycosylation engineering of Chinese hamster ovary (CHO) cells. Biotechnol Bioeng 59:455-450.
    • (1998) Biotechnol Bioeng , vol.59 , pp. 455-1450
    • Prati, E.G.P.1    Scheidegger, P.2    Sburiati, A.R.3    Bailey, J.E.4
  • 63
    • 0023645520 scopus 로고
    • Carbohydrate structure of erythropoietin expressed in Chinese hamster ovary cells by a human erythropoietin cDNA
    • Saski H, Bothner B, Dell A, Fukuda M. 1987. Carbohydrate structure of erythropoietin expressed in Chinese hamster ovary cells by a human erythropoietin cDNA. J Biol Chem 262:12059-12076.
    • (1987) J Biol Chem , vol.262 , pp. 12059-12076
    • Saski, H.1    Bothner, B.2    Dell, A.3    Fukuda, M.4
  • 64
    • 0032032778 scopus 로고    scopus 로고
    • Synthesis of bisected glycoforms of recombinant IFN-γ by overexpression of β-1,4-N-acetylglucosaminyltransferase III in Chinese hamster ovary cells
    • Sburiati AR, Umana P, Prati EGP, Bailey JE. 1998. Synthesis of bisected glycoforms of recombinant IFN-γ by overexpression of β-1,4-N-acetylglucosaminyltransferase III in Chinese hamster ovary cells. Biotechnol Prog 14:189-192.
    • (1998) Biotechnol Prog , vol.14 , pp. 189-192
    • Sburiati, A.R.1    Umana, P.2    Prati, E.G.P.3    Bailey, J.E.4
  • 65
    • 0025726319 scopus 로고
    • Carbohydrate structure of recombinant soluble human CD4 expressed in Chinese hamster ovary cells
    • Spellman MW, Leonard CK, Basa LJ. 1991. Carbohydrate structure of recombinant soluble human CD4 expressed in Chinese hamster ovary cells. Biochemistry 30:2395-2406.
    • (1991) Biochemistry , vol.30 , pp. 2395-2406
    • Spellman, M.W.1    Leonard, C.K.2    Basa, L.J.3
  • 66
    • 0031554618 scopus 로고    scopus 로고
    • Increasing GPI-anchored protein harvest concentrations from suspension and porous microcarrier CHO cell cultures
    • Sunderji R, Kennard ML, Piret JM. 1997. Increasing GPI-anchored protein harvest concentrations from suspension and porous microcarrier CHO cell cultures. Biotechnol Bioeng 55:136-147.
    • (1997) Biotechnol Bioeng , vol.55 , pp. 136-147
    • Sunderji, R.1    Kennard, M.L.2    Piret, J.M.3
  • 67
    • 0027517557 scopus 로고
    • Purification and characterization of recombinunt human thyrotropin (TSH) isoforms produced by Chinese hamster ovary cells: The role of sialylation and sulfution in TSH bioactivity
    • Szkudlinski MW, Thotakura NR, Bucci I, Joshi LR, Tsai A, East-Palmer J, Shiloach J, Weintraub BD. 1993. Purification and characterization of recombinunt human thyrotropin (TSH) isoforms produced by Chinese hamster ovary cells: The role of sialylation and sulfution in TSH bioactivity. Endocrinology 123:1490-1503.
    • (1993) Endocrinology , vol.123 , pp. 1490-1503
    • Szkudlinski, M.W.1    Thotakura, N.R.2    Bucci, I.3    Joshi, L.R.4    Tsai, A.5    East-Palmer, J.6    Shiloach, J.7    Weintraub, B.D.8
  • 68
    • 0028243819 scopus 로고
    • Structural studies of a novel type pentaantennary large glycan unit in the fertilization-associated carbohydrate-rich glycopeptide isolated from fertilized eggs of Oryzias latipes
    • Taguchi T, Seko A, Kitajima K, Muto Y, Inoue S, Khoo KH, Morris HR, Dell A, lnoue Y. 1994. Structural studies of a novel type pentaantennary large glycan unit in the fertilization-associated carbohydrate-rich glycopeptide isolated from fertilized eggs of Oryzias latipes. J Biol Chem 269:8762-8771.
    • (1994) J Biol Chem , vol.269 , pp. 8762-8771
    • Taguchi, T.1    Seko, A.2    Kitajima, K.3    Muto, Y.4    Inoue, S.5    Khoo, K.H.6    Morris, H.R.7    Dell, A.8    Lnoue, Y.9
  • 69
    • 0023849601 scopus 로고
    • Comparative study of the asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells
    • Takeuchi M, et al. 1988. Comparative study of the asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells. J Biol Chem 263:3657-3663.
    • (1988) J Biol Chem , vol.263 , pp. 3657-3663
    • Takeuchi, M.1
  • 70
    • 0343863817 scopus 로고
    • Relationships between sugar chain structure and biological activity of recombinant human erythropoietin produced in Chinese hamster ovary cells
    • Takeuchi M, Inoue N, Strickland TW, Kubota M, Wada M, Shizu R, Hoshi S, Kozutsumi H, Takasaki S, Kobata A. 1989. Relationships between sugar chain structure and biological activity of recombinant human erythropoietin produced in Chinese hamster ovary cells. J Biol Chem 263.3657-3663.
    • (1989) J Biol Chem , vol.263 , pp. 3657-3663
    • Takeuchi, M.1    Inoue, N.2    Strickland, T.W.3    Kubota, M.4    Wada, M.5    Shizu, R.6    Hoshi, S.7    Kozutsumi, H.8    Takasaki, S.9    Kobata, A.10
  • 71
    • 0027318961 scopus 로고
    • Biological role of oligosaccharides: All of the theories are correct
    • Varki A. 1993. Biological role of oligosaccharides: All of the theories are correct. Glycobiology 2:97-130.
    • (1993) Glycobiology , vol.2 , pp. 97-130
    • Varki, A.1
  • 72
    • 0028185911 scopus 로고
    • The major glycosylation pathways of mammalian membranes a summary
    • Maddy AH, Harris JR, editors. New York: Plenum Press
    • Varki A, Freeze H. 1994. The major glycosylation pathways of mammalian membranes a summary. In: Maddy AH, Harris JR, editors. Subcellular biochemistry: Membrane biogenesis. New York: Plenum Press. p 71-100.
    • (1994) Subcellular Biochemistry: Membrane Biogenesis , pp. 71-100
    • Varki, A.1    Freeze, H.2
  • 73
    • 0028931761 scopus 로고
    • Stable secretion of a soluble, oligomeric form of the rabies virus glycoprotein: Influence of N-glycan processing on secretion
    • Wojezyk B, Shakin-Eshleman SH, Doms RW, Xiang Z, Hildegund CJE, Wunner W, Spitalnik SL. 1995. Stable secretion of a soluble, oligomeric form of the rabies virus glycoprotein: Influence of N-glycan processing on secretion. Biochemistry 34:2599-2609.
    • (1995) Biochemistry , vol.34 , pp. 2599-2609
    • Wojezyk, B.1    Shakin-Eshleman, S.H.2    Doms, R.W.3    Xiang, Z.4    Hildegund, C.J.E.5    Wunner, W.6    Spitalnik, S.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.