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Volumn 14, Issue 8, 1996, Pages 975-981

Getting the glycosylation right: Implications for the biotechnology industry

Author keywords

Antigenicity; Carbohydrates; Clearance; Glycosylation; Recombinant; Review

Indexed keywords

GLYCOSYLTRANSFERASE;

EID: 0029837484     PISSN: 10870156     EISSN: 15461696     Source Type: Journal    
DOI: 10.1038/nbt0896-975     Document Type: Article
Times cited : (389)

References (106)
  • 1
    • 0026701647 scopus 로고
    • Glycoprotein glycans—roles and controls
    • Geisow, M.J. 1992. Glycoprotein glycans—roles and controls. Trends Biotechnol. 10:333-335.
    • (1992) Trends Biotechnol , vol.10 , pp. 333-335
    • Geisow, M.J.1
  • 2
    • 0026848764 scopus 로고
    • Glycoprotein pharmaceuticals—scientific and regulatory considerations, and the United-States Orphan Drug-Act
    • Liu, D.T.Y. 1992. Glycoprotein pharmaceuticals—scientific and regulatory considerations, and the United-States Orphan Drug-Act. Trends Biotechnol. 10:114-120.
    • (1992) Trends Biotechnol , vol.10 , pp. 114-120
    • Liu, D.T.Y.1
  • 3
    • 0026505331 scopus 로고
    • Topography of glycosylation reactions in the endoplasmic reticulum
    • Abeijon, C. and Hirschberg, C.B. 1992. Topography of glycosylation reactions in the endoplasmic reticulum. Trends Biochem. Sci. 17:32-36.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 32-36
    • Abeijon, C.1    Hirschberg, C.B.2
  • 5
    • 0026687937 scopus 로고
    • Mammalian glycosyltransferases: Genomic organization and protein structure
    • Joziasse, D.H. 1992. Mammalian glycosyltransferases: genomic organization and protein structure. Glycobiology 2:271-277.
    • (1992) Glycobiology , vol.2 , pp. 271-277
    • Joziasse, D.H.1
  • 6
    • 0029144380 scopus 로고
    • Molecular-cloning of eukaryotic glycoprotein and glycolipid glycosyltransferases—a survey
    • Field, M.C. and Wainwright, L.J. 1995. Molecular-cloning of eukaryotic glycoprotein and glycolipid glycosyltransferases—a survey. Glycobiology 5:463-472.
    • (1995) Glycobiology , vol.5 , pp. 463-472
    • Field, M.C.1    Wainwright, L.J.2
  • 7
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. 1993. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3:97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 8
    • 0026640805 scopus 로고
    • Comparing the glycosylation patterns of recombinant glycoproteins
    • Parekh, R.B. and Patel, T.P. 1992. Comparing the glycosylation patterns of recombinant glycoproteins. Trends Biotechnol. 10:276-280.
    • (1992) Trends Biotechnol , vol.10 , pp. 276-280
    • Parekh, R.B.1    Patel, T.P.2
  • 9
    • 0028224656 scopus 로고
    • Glycosylation of recombinant proteins: Problems and prospects
    • Jenkins, N. and Curling, E.M. 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, E.M.2
  • 10
    • 11944272604 scopus 로고
    • Environmental effects on protein glycosylation
    • Goochee, C.F. and Monica, T.J. 1990. Environmental effects on protein glycosylation. Bio/Technology 8:421-427.
    • (1990) Bio/Technology , vol.8 , pp. 421-427
    • Goochee, C.F.1    Monica, T.J.2
  • 11
    • 0025840338 scopus 로고
    • The oligosaccharides of glycoproteins—bioprocess factors affecting oligosaccharide structure and their effect on glycoprotein properties
    • Goochee, C.F., Gramer, M.J., Andersen, D.C., Bahr, J.B., and Rasmussen, J.R. 1991. The oligosaccharides of glycoproteins—bioprocess factors affecting oligosaccharide structure and their effect on glycoprotein properties. Bio/Technology 9:1347-1355.
    • (1991) Bio/Technology , vol.9 , pp. 1347-1355
    • Goochee, C.F.1    Gramer, M.J.2    Ersen, D.C.3    Bahr, J.B.4    Rasmussen, J.R.5
  • 12
    • 0028928202 scopus 로고
    • Glycosylation of human truncated Fc-epsilon-RI α-chain is necessary for efficient folding in the endoplasmic-reticulum
    • Letourneur, O., Sechi, S., Willettebrown, J., Robertson, M.W., and Kinet, J.P. 1995. Glycosylation of human truncated Fc-epsilon-RI α-chain is necessary for efficient folding in the endoplasmic-reticulum. J. Biol. Chem. 270:8249-8256.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8249-8256
    • Letourneur, O.1    Sechi, S.2    Willettebrown, J.3    Robertson, M.W.4    Kinet, J.P.5
  • 13
    • 0028840449 scopus 로고
    • Meningococcal pilin—a glycoprotein substituted with digalactosyl 2, 4-diacetamido-2, 4, 6-trideoxyhexose
    • Stimson, E., Virji, M., Makepeace, K., Dell, A., Morris, H.R., Payne, G., et al. 1995. Meningococcal pilin—a glycoprotein substituted with digalactosyl 2, 4-diacetamido-2, 4, 6-trideoxyhexose. Mol. Microbiol. 17:1201-1214.
    • (1995) Mol. Microbiol. , vol.17 , pp. 1201-1214
    • Stimson, E.1    Virji, M.2    Makepeace, K.3    Dell, A.4    Morris, H.R.5    Payne, G.6
  • 14
    • 0027402074 scopus 로고
    • Glycoprotein biosynthesis in yeast
    • Herscovics, A.O. and Orlean, P. 1993. Glycoprotein biosynthesis in yeast. FASEB J. 7:540-550.
    • (1993) FASEB J , vol.7 , pp. 540-550
    • Herscovics, A.O.1    Orlean, P.2
  • 15
    • 0028025347 scopus 로고
    • Characterization and evaluation of a recombinant hepatitis-B vaccine expressed in yeast defective for N-linked hyperglycosylation
    • Kniskern, P.J., Hagopian, A., Burke, P., Schulz, L.D., Montgomery, D.L., Hurni, W.M., et al. 1994. Characterization and evaluation of a recombinant hepatitis-B vaccine expressed in yeast defective for N-linked hyperglycosylation. Vaccine 12:1021-1025.
    • (1994) Vaccine , vol.12 , pp. 1021-1025
    • Kniskern, P.J.1    Hagopian, A.2    Burke, P.3    Schulz, L.D.4    Montgomery, D.L.5    Hurni, W.M.6
  • 16
    • 0029091130 scopus 로고
    • Glycoprotein-biosynthesis in Saccharomyces cerevisiae—ngd29, an N-glyco-sylation mutant allelic to och1 having a defect in the initiation of outer chain formation
    • Lehle, L., Eiden, A., Lehnert, K., Haselbeck, A., and Kopetzki, E. 1995. Glycoprotein-biosynthesis in Saccharomyces cerevisiae—ngd29, an N-glyco-sylation mutant allelic to och1 having a defect in the initiation of outer chain formation. FEBS Lett. 370:41-45.
    • (1995) FEBS Lett , vol.370 , pp. 41-45
    • Lehle, L.1    Eiden, A.2    Lehnert, K.3    Haselbeck, A.4    Kopetzki, E.5
  • 17
    • 0026767246 scopus 로고
    • Comparison of the carbohydrate moieties of recombinant soluble Fc-epsilon receptor (SFc-Î-Rll/scd23) expressed in Saccharomyces cerevisiae and chinese hamster ovary cells—different O-glycosylation sites are used by yeast and mammalian cells
    • Kalsner, I., Schneider, F.J., Geyer, R., Ahorn, H., and Maurerfogy, I. 1992. Comparison of the carbohydrate moieties of recombinant soluble Fc-epsilon receptor (sFc-Î-Rll/scd23) expressed in Saccharomyces cerevisiae and chinese hamster ovary cells—different O-glycosylation sites are used by yeast and mammalian cells. Glycoconjugate J. 9:209-216.
    • (1992) Glycoconjugate J , vol.9 , pp. 209-216
    • Kalsner, I.1    Schneider, F.J.2    Geyer, R.3    Ahorn, H.4    Maurerfogy, I.5
  • 18
    • 0029257224 scopus 로고
    • Characterization of a human glycoprotein (Erythropoietin) produced in cultured tobacco cells
    • Matsurnoto, S., Ikura, K., Ueda, M., and Sasaki, R. 1995. Characterization of a human glycoprotein (erythropoietin) produced in cultured tobacco cells. Plant Mol. Biol. 27:1163-1172.
    • (1995) Plant Mol. Biol. , vol.27 , pp. 1163-1172
    • Matsurnoto, S.1    Ikura, K.2    Ueda, M.3    Sasaki, R.4
  • 19
    • 0343288749 scopus 로고
    • Fucose in α1-3 linkage to the N-glycan core forms an allergenic epitope that occurs in plant and in insect glycoproteins
    • Altmann, F., Tretter, V., Kubelka, V., Staudacher, E., Marz, L., and Becker, W.M. 1993. Fucose in α1-3 linkage to the N-glycan core forms an allergenic epitope that occurs in plant and in insect glycoproteins. Glycoconjugate J. 10:301.
    • (1993) Glycoconjugate J , vol.10 , pp. 301
    • Altmann, F.1    Tretter, V.2    Kubelka, V.3    Staudacher, E.4    Marz, L.5    Becker, W.M.6
  • 20
    • 0029411968 scopus 로고
    • Immunotherapeutic potential of antibodies produced in plants
    • Ma, J.K.C. and Hein, M.B. 1995. Immunotherapeutic potential of antibodies produced in plants. Trends Biotechnol. 13:522-527.
    • (1995) Trends Biotechnol , vol.13 , pp. 522-527
    • Ma, J.K.C.1    Hein, M.B.2
  • 21
    • 0029065680 scopus 로고
    • N-glycosylation of recombinant human interferon-γ produced in different animal expression systems
    • James, D.C., Freedman, R.B., Hoare, M., Ogonah, O.W., Rooney, B.C., Larionov, O.A., et al. 1995. N-glycosylation of recombinant human interferon-γ produced in different animal expression systems. Bio/Technology 13:592-596.
    • (1995) Bio/Technology , vol.13 , pp. 592-596
    • James, D.C.1    Freedman, R.B.2    Hoare, M.3    Ogonah, O.W.4    Rooney, B.C.5    Larionov, O.A.6
  • 22
    • 0027296753 scopus 로고
    • Biosynthesis and secretion of human interleukin-2 glycoprotein variants from baculovirus-infected sf21 cells—characterization of polypeptides and post-translational modifications
    • Grabenhorst, E., Hofer, B., Nimtz, M., Jager, V., and Conradt, H.S. 1993. Biosynthesis and secretion of human interleukin-2 glycoprotein variants from baculovirus-infected sf21 cells—characterization of polypeptides and post-translational modifications. Eur. J. Biochem. 215:189-197.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 189-197
    • Grabenhorst, E.1    Hofer, B.2    Nimtz, M.3    Jager, V.4    Conradt, H.S.5
  • 23
    • 0028789632 scopus 로고
    • Biochemical-analysis of the N-glycosylation pathway in baculovirus-infected lepidopteran insect cells
    • Jarvis, D.L. and Finn, E.E. 1995. Biochemical-analysis of the N-glycosylation pathway in baculovirus-infected lepidopteran insect cells. Virology 212:500-511.
    • (1995) Virology , vol.212 , pp. 500-511
    • Jarvis, D.L.1    Finn, E.E.2
  • 24
    • 0025336176 scopus 로고
    • Oligosaccharide processing in the expression of human plasminogen cDNA by lepidopteran insect (Spodoptera frugiperda) cells
    • Davidson, D.J.C., Fraser, M.J., and Castellino, F.J. 1990. Oligosaccharide processing in the expression of human plasminogen cDNA by lepidopteran insect (Spodoptera frugiperda) cells. Biochemistry 29:5584-5590.
    • (1990) Biochemistry , vol.29 , pp. 5584-5590
    • Davidson, D.J.C.1    Fraser, M.J.2    Castellino, F.J.3
  • 25
    • 0030070842 scopus 로고    scopus 로고
    • Isolation and characterization of an insect-cell line able to perform complex N-linked glycosylation on recombinant proteins
    • Ogonah, O.W., Freedman, R.B., Jenkins, N., Patel, K., and Rooney, B.C. 1996. Isolation and characterization of an insect-cell line able to perform complex N-linked glycosylation on recombinant proteins. Bio/Technology 14:197-202.
    • (1996) Bio/Technology , vol.14 , pp. 197-202
    • Ogonah, O.W.1    Freedman, R.B.2    Jenkins, N.3    Patel, K.4    Rooney, B.C.5
  • 26
    • 0028793359 scopus 로고
    • Intrinsic glycosylation potentials of insect-cell cultures and insect larvae
    • Davis, T.R. and Wood, H.A. 1995. Intrinsic glycosylation potentials of insect-cell cultures and insect larvae. In Vitro Cellular Develop. Biol.-Animal 31:659-663.
    • (1995) Vitro Cellular Develop. Biol.-Animal , vol.31 , pp. 659-663
    • Davis, T.R.1    Wood, H.A.2
  • 27
    • 0025264624 scopus 로고
    • Frameshift and nonsense mutations in a human genomic sequence homologous to a murine UDP-Gal:ß-D-Gal(1, 4)-D-GlcNAc α(1, 3)-galactosyl-transferase cDNA
    • Larsen, R.D., Rivera-Marrero, C.A., Ernst, L.K., Cummings, R.D., and Lowe, J.B. 1990. Frameshift and nonsense mutations in a human genomic sequence homologous to a murine UDP-Gal:ß-D-Gal(1, 4)-D-GlcNAc α(1, 3)-galactosyl-transferase cDNA. J. Biol. Chem. 265:7055-7061.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7055-7061
    • Larsen, R.D.1    Rivera-Marrero, C.A.2    Ernst, L.K.3    Cummings, R.D.4    Lowe, J.B.5
  • 28
    • 0027485672 scopus 로고
    • Does endogenous glycosylation prevent the use of mouse monoclonal antibodies as cancer therapeutics?
    • Borrebaeck, C.A.K., Malmborg, A.C., and Ohlin, M. 1993. Does endogenous glycosylation prevent the use of mouse monoclonal antibodies as cancer therapeutics? Immunol. Today 14:477-479.
    • (1993) Immunol. Today , vol.14 , pp. 477-479
    • Borrebaeck, C.A.K.1    Malmborg, A.C.2    Ohlin, M.3
  • 29
    • 0025111377 scopus 로고
    • Specificity of human natural antibody to recombinant tissue-type plasminogen activator (T-PA) expressed in mouse C127 cells
    • Tsuji, J., Noma, S., Suzuki, J., Okumura, K., and Shimizu, N. 1990. Specificity of human natural antibody to recombinant tissue-type plasminogen activator (t-PA) expressed in mouse C127 cells. Chem. Pharm. Bull. 38:765-768.
    • (1990) Chem. Pharm. Bull. , vol.38 , pp. 765-768
    • Tsuji, J.1    Noma, S.2    Suzuki, J.3    Okumura, K.4    Shimizu, N.5
  • 30
    • 0027526023 scopus 로고
    • Glycosylation of human IgG subclass and mouse lgG2b heavy chains secreted by mouse J558L transfectoma cell lines as chimeric antibodies
    • Lund, J.T., Takahashi, N., Hindley, S.A., Tyler, R., Goodall, M., and Jefferis, R. 1993. Glycosylation of human IgG subclass and mouse lgG2b heavy chains secreted by mouse J558L transfectoma cell lines as chimeric antibodies. Human Antibodies & Hybridomas 4:20-25.
    • (1993) Human Antibodies & Hybridomas , vol.4 , pp. 20-25
    • Lund, J.T.1    Takahashi, N.2    Hindley, S.A.3    Tyler, R.4    Goodall, M.5    Jefferis, R.6
  • 31
    • 0027319101 scopus 로고
    • Control of IgG/Fc glycosylation: A comparison of oligosaccharides from chimeric human/mouse and mouse subclass immunoglobulin Gs
    • Lund, J.T., Takahashi, N., Nakagawa, H., Goodall, M., Bentley, T., Hindley, S.A., et al. 1993. Control of IgG/Fc glycosylation: a comparison of oligosaccharides from chimeric human/mouse and mouse subclass immunoglobulin Gs. Mol. Immunol. 30:741-748.
    • (1993) Mol. Immunol. , vol.30 , pp. 741-748
    • Lund, J.T.1    Takahashi, N.2    Nakagawa, H.3    Goodall, M.4    Bentley, T.5    Hindley, S.A.6
  • 33
    • 0029563888 scopus 로고
    • Glycosylation and biological activity of CAMPATH-1H expressed in different cell lines and grown under different culture conditions
    • Lifely, M.R., Hale, C., Boyce, S., Keen, M.J., and Phillips, J. 1995. Glycosylation and biological activity of CAMPATH-1H expressed in different cell lines and grown under different culture conditions. Glycobiology 5:813-822.
    • (1995) Glycobiology , vol.5 , pp. 813-822
    • Lifely, M.R.1    Hale, C.2    Boyce, S.3    Keen, M.J.4    Phillips, J.5
  • 34
    • 0029162562 scopus 로고
    • Comprehensive pharmacokinetics of a humanized antibody and analysis of residual anti-idiotypic responses
    • Stephens, S., Emtage, S., Vetterlein, O., Chaplin, L., Bebbington, C., Nesbitt, A., et al. 1995. Comprehensive pharmacokinetics of a humanized antibody and analysis of residual anti-idiotypic responses. Immunology 85:668-674.
    • (1995) Immunology , vol.85 , pp. 668-674
    • Stephens, S.1    Emtage, S.2    Vetterlein, O.3    Chaplin, L.4    Bebbington, C.5    Nesbitt, A.6
  • 35
    • 0028800079 scopus 로고
    • Glycosylation of the variable region of immunoglobulin G: Site-specific maturation of the sugar chains
    • Endo, T., Wright, A., Morrison, S.L., and Kobata, A. 1995. Glycosylation of the variable region of immunoglobulin G: site-specific maturation of the sugar chains. Mol. Immunol. 32:931-940.
    • (1995) Mol. Immunol. , vol.32 , pp. 931-940
    • Endo, T.1    Wright, A.2    Morrison, S.L.3    Kobata, A.4
  • 36
    • 0026697011 scopus 로고
    • Human natural anti-Gal IgG regulates alternative complement pathway activation on bacterial surfaces
    • Hamadeh, R.M., Jarvis, G.A., Galili, U., Mandrell, R.E., Zhou, P., and Griffiss, J.M. 1992. Human natural anti-Gal IgG regulates alternative complement pathway activation on bacterial surfaces. J. Clin. Invest. 89:1223-1235.
    • (1992) J. Clin. Invest. , vol.89 , pp. 1223-1235
    • Hamadeh, R.M.1    Jarvis, G.A.2    Galili, U.3    Mandrell, R.E.4    Zhou, P.5    Griffiss, J.M.6
  • 37
    • 0028805535 scopus 로고
    • Enzymatic removal of α-galactosyl epitopes from porcine endothelial-cells diminishes the cytotoxic effect of natural antibodies
    • Lavecchio, J.A., Dunne, A.D., and Edge, A.S.B. 1995. Enzymatic removal of α-galactosyl epitopes from porcine endothelial-cells diminishes the cytotoxic effect of natural antibodies. Transplantation 60:841-847.
    • (1995) Transplantation , vol.60 , pp. 841-847
    • Lavecchio, J.A.1    Dunne, A.D.2    Edge, A.S.B.3
  • 38
    • 0028952933 scopus 로고
    • Characterization of the glycosylation of a human-IgM produced by a human-mouse hybridoma
    • Monica, T.J., Williams, S.B., Goochee, C.F., and Maiorella, B.L. 1995. Characterization of the glycosylation of a human-IgM produced by a human-mouse hybridoma. Glycobiology 5:175-185.
    • (1995) Glycobiology , vol.5 , pp. 175-185
    • Monica, T.J.1    Williams, S.B.2    Goochee, C.F.3    Maiorella, B.L.4
  • 39
    • 0024391058 scopus 로고
    • Biosynthesis of N-glycolyneuraminic acid. The primary site of hydroxylation of N-acetyl-neuraminic acid is the cytosolic sugar nucleotide pool
    • Muchmore, E.A., Milewski, M., Varki, A., and Diaz, S. 1989. Biosynthesis of N-glycolyneuraminic acid. The primary site of hydroxylation of N-acetyl-neuraminic acid is the cytosolic sugar nucleotide pool. J. Biol. Chem. 264:20216-20223.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20216-20223
    • Muchmore, E.A.1    Milewski, M.2    Varki, A.3    Diaz, S.4
  • 40
    • 0028798520 scopus 로고
    • Immunogenicity of N-glycolylneuraminic acid-containing carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells
    • Noguchi, A., Mukuria, C.J., Suzuki, E., and Naiki, M. 1995. Immunogenicity of N-glycolylneuraminic acid-containing carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. J. Biochem. 117:59-62.
    • (1995) J. Biochem. , vol.117 , pp. 59-62
    • Noguchi, A.1    Mukuria, C.J.2    Suzuki, E.3    Naiki, M.4
  • 41
    • 0029636508 scopus 로고
    • Fluorophore labeled glycan analysis of immunoglobulin fusion proteins: Correlation of oligosaccharide content with in vivo clearance profile
    • Flesher, A.R., Marzowski, J., Wang, W.C., and Raff, H.V. 1995. Fluorophore labeled glycan analysis of immunoglobulin fusion proteins: correlation of oligosaccharide content with in vivo clearance profile. Biotechnol. Bioeng. 46:399-407.
    • (1995) Biotechnol. Bioeng. , vol.46 , pp. 399-407
    • Flesher, A.R.1    Marzowski, J.2    Wang, W.C.3    Raff, H.V.4
  • 42
    • 0029000263 scopus 로고
    • Molecular cloning of cytidine monophospho-N-acetylneuraminic acid hydroxylase: Regulation of species-specific and tissue-specific expression of N-glycolylneuraminic acid
    • Kawano, T., Koyama, S., Takematsu, H., Kozutsumi, Y., Kawasaki, H., Kawashima, S., et al. 1995. Molecular cloning of cytidine monophospho-N-acetylneuraminic acid hydroxylase: regulation of species-specific and tissue-specific expression of N-glycolylneuraminic acid. J. Biol. Chem. 270:16458-16463.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16458-16463
    • Kawano, T.1    Koyama, S.2    Takematsu, H.3    Kozutsumi, Y.4    Kawasaki, H.5    Kawashima, S.6
  • 43
    • 0025240089 scopus 로고
    • Transfer and expression of a murine UDP-Gal:ß-D-Gal-α1, 3-galactosyltransferase gene in transfected Chinese hamster ovary cells. Competition reactions between the α1, 3-galactosyltransferase and the endogenous α2, 3-sialyltransferase
    • Smith, D.F., Larsen, R.D., Mattox, S.A., Lowe, J.B., and Cummings, R.D. 1990, Transfer and expression of a murine UDP-Gal:ß-D-Gal-α1, 3-galactosyltransferase gene in transfected Chinese hamster ovary cells. Competition reactions between the α1, 3-galactosyltransferase and the endogenous α2, 3-sialyltransferase. J. Biol. Chem. 265:6225-6234.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6225-6234
    • Smith, D.F.1    Larsen, R.D.2    Mattox, S.A.3    Lowe, J.B.4    Cummings, R.D.5
  • 44
    • 0028957067 scopus 로고
    • Structural-analysis of the sialylated N-linked and O-linked carbohydrate chains of recombinant-human-erythropoietin expressed in chinese-hamster ovary cells—sialylation patterns and branch location of dimeric N-acetyllactosamine units
    • Hokke, C.H., Bergwerff, A.A., Vandedem, G.W.K., Kamerling, J.P., and Vliegenthart, J.F.G. 1995. Structural-analysis of the sialylated N-linked and O-linked carbohydrate chains of recombinant-human-erythropoietin expressed in chinese-hamster ovary cells—sialylation patterns and branch location of dimeric N-acetyllactosamine units. Eur. J. Biochem. 228:981-1008.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 981-1008
    • Hokke, C.H.1    Bergwerff, A.A.2    Vandedem, G.W.K.3    Kamerling, J.P.4    Vliegenthart, J.F.G.5
  • 45
    • 0024321508 scopus 로고
    • Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of ß-galactoside α2, 6-sialyltransferase
    • Lee, E.U., Roth, J., and Paulson, J.C. 1989. Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of ß-galactoside α2, 6-sialyltransferase. J. Biol. Chem. 264:13848-13855.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13848-13855
    • Lee, E.U.1    Roth, J.2    Paulson, J.C.3
  • 46
    • 0029294124 scopus 로고
    • Tissue-plasminogen activator co-expressed in chinese-hamster ovary cells with α2, 6-sialyltransferase contains NeuAc-α2, 6gal-ß1, 4GlcNAc linkages
    • Minch, S.L., Kallio, P.T., and Bailey, J.E. 1995. Tissue-plasminogen activator co-expressed in chinese-hamster ovary cells with α2, 6-sialyltransferase contains NeuAc-α2, 6gal-ß1, 4GlcNAc 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
  • 47
    • 0028979967 scopus 로고
    • Construction of stable BHK-21-cells coexpressing human secretory glycoproteins and human Gal(ß-1-4)GlcNAc-r α-2, 6-sialyltransferase α-2, 6-linked NeuAc is preferentially attached to the Gal(ß-1-4)GlcNAc(ß-1-2)Man(α-1-3)-branch of diantennary oligosaccharides from secreted recombinant ß-trace protein
    • Grabenhorst, E., Hoffmann, A., Nimtz, M., Zettlmeissl, G., and Conradt, H.S. 1995. Construction of stable BHK-21-cells coexpressing human secretory glycoproteins and human Gal(ß-1-4)GlcNAc-r α-2, 6-sialyltransferase α-2, 6-linked NeuAc is preferentially attached to the Gal(ß-1-4)GlcNAc(ß-1-2)Man(α-1-3)-branch of diantennary oligosaccharides from secreted recombinant ß-trace protein. Eur. J. Biochem. 232:718-725.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 718-725
    • Grabenhorst, E.1    Hoffmann, A.2    Nimtz, M.3    Zettlmeissl, G.4    Conradt, H.S.5
  • 48
    • 0028845998 scopus 로고
    • Glycosyltransferase mutants—key to new insights in glycobiology
    • Stanley, P. and Ioffe, E. 1995. Glycosyltransferase mutants—key to new insights in glycobiology. FASEB J. 9:1436-1444.
    • (1995) FASEB J , vol.9 , pp. 1436-1444
    • Stanley, P.1    Ioffe, E.2
  • 49
    • 0024562457 scopus 로고
    • Altered glycosylation of serum transferrin of patients with hepatocellular carcinoma
    • Yamashita, K., Koide, N., Endo, T., Iwaki, Y., and Kobata, A. 1989. Altered glycosylation of serum transferrin of patients with hepatocellular carcinoma. J. Biol. Chem. 264:2415-2423.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2415-2423
    • Yamashita, K.1    Koide, N.2    Endo, T.3    Iwaki, Y.4    Kobata, A.5
  • 50
    • 18544408875 scopus 로고
    • N-linked glycosylation of tissue-plasminogen activator in Namalwa cells
    • Khan, M.W., Musgrave, S.C., and Jenkins, N. 1995. N-linked glycosylation of tissue-plasminogen activator in Namalwa cells. Biochem. Soc. Trans. 23:S99.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. S99
    • Khan, M.W.1    Musgrave, S.C.2    Jenkins, N.3
  • 51
    • 0025854919 scopus 로고
    • Purification and characterization of three forms of differently glycosylated recombinant human granulocyte-macrophage colony-stimulating factor
    • Okamoto, M., Nakai, M., Nakayama, C., Yanagi, H., Matsui, H., Noguchi, H., et al. 1991. Purification and characterization of three forms of differently glycosylated recombinant human granulocyte-macrophage colony-stimulating factor. Arch. Biochem. Biophys. 286:562-568.
    • (1991) Arch. Biochem. Biophys. , vol.286 , pp. 562-568
    • Okamoto, M.1    Nakai, M.2    Nakayama, C.3    Yanagi, H.4    Matsui, H.5    Noguchi, H.6
  • 52
    • 0026337655 scopus 로고
    • Structural study of the sugar moieties of monoclonal antibodies secreted by human-mouse hybridoma
    • Tandai, M., Endo, T., Sasaki, S., Masuho, Y., Kochibe, N., and Kobata, A. 1991. Structural study of the sugar moieties of monoclonal antibodies secreted by human-mouse hybridoma. Arch. Biochem. Biophys. 291:339-348.
    • (1991) Arch. Biochem. Biophys. , vol.291 , pp. 339-348
    • Tandai, M.1    Endo, T.2    Sasaki, S.3    Masuho, Y.4    Kochibe, N.5    Kobata, A.6
  • 53
    • 0009719139 scopus 로고
    • Glycosylation patterns of human proteins expressed in transgenic goat milk
    • Cole, E.S., Higgins, E., Bernasconi, R., Garone, L., and Edmunds, T. 1994. Glycosylation patterns of human proteins expressed in transgenic goat milk. J. Cell Biochem. 265:S18D.
    • (1994) J. Cell Biochem. , vol.265 , pp. S18D
    • Cole, E.S.1    Higgins, E.2    Bernasconi, R.3    Garone, L.4    Edmunds, T.5
  • 54
    • 0028883995 scopus 로고
    • Remodeling of mouse milk glycoconjugates by transgenic expression of a human glycosyltransferase
    • Prieto, P.A., Mukerji, P., Kelder, B., Erney, R., Gonzalez, D., Yun, J.S., et al. 1995. Remodeling of mouse milk glycoconjugates by transgenic expression of a human glycosyltransferase. J. Biol. Chem. 270:29515-29519.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29515-29519
    • Prieto, P.A.1    Mukerji, P.2    Kelder, B.3    Erney, R.4    Gonzalez, D.5    Yun, J.S.6
  • 55
    • 0028826728 scopus 로고
    • Transfection of N-acetylglucosaminyltransferase-III gene suppresses expression of hepatitis-B virus in a human hepatoma-cell line, HB611
    • Miyoshi, E., Ihara, Y., Hayashi, N., Fusamoto, H., Kamada, T., and Taniguchi, N. 1995. Transfection of N-acetylglucosaminyltransferase-III gene suppresses expression of hepatitis-B virus in a human hepatoma-cell line, HB611. J. Biol. Chem. 270:28311-28315.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28311-28315
    • Miyoshi, E.1    Ihara, Y.2    Hayashi, N.3    Fusamoto, H.4    Kamada, T.5    Taniguchi, N.6
  • 57
    • 0028244694 scopus 로고
    • Agalactosyl glycoforms of IgG autoantibodies are pathogenic
    • Rademacher, T.W., Williams, P., and Dwek, R.A. 1994. Agalactosyl glycoforms of IgG autoantibodies are pathogenic. Proc. Natl. Acad. Sci. USA 91:6123-6127.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6123-6127
    • Rademacher, T.W.1    Williams, P.2    Dwek, R.A.3
  • 58
    • 0028174037 scopus 로고
    • 4-4GalNAc-ß1, 4GlcNAc-ß-1, which is the archetypal nonreducing epitope in the N-glycans of pituitary glycohormones
    • 4-4GalNAc-ß1, 4GlcNAc-ß-1, which is the archetypal nonreducing epitope in the N-glycans of pituitary glycohormones. J. Biol. Chem. 269:910-920.
    • (1994) J. Biol. Chem. , vol.269 , pp. 910-920
    • Siciliano, R.A.1    Morris, H.R.2    Bennett, H.P.J.3    Dell, A.4
  • 59
    • 0028908612 scopus 로고
    • The major N-linked carbohydrate chains from human urokinase—the occurrence of 4-O-sulfated, (α2, 6)-sialylated or (α-1, 3)-fucosylated N-acetylgalactosamine(ß-1-4)-N-acetylglucosamine elements
    • Bergwerff, A.A., Vanoostrum, J., Kamerling, J.P., and Vliegenthart, J.F.G. 1995. The major N-linked carbohydrate chains from human urokinase—the occurrence of 4-O-sulfated, (α2, 6)-sialylated or (α-1, 3)-fucosylated N-acetylgalactosamine(ß-1-4)-N-acetylglucosamine elements. Eur. J. Biochem. 228:1009-1019.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 1009-1019
    • Bergwerff, A.A.1    Vanoostrum, J.2    Kamerling, J.P.3    Vliegenthart, J.F.G.4
  • 61
    • 0026604570 scopus 로고
    • Molecular basis of recognition by the glycoprotein hormone-specific N-acetylgalactosamine-transferase
    • Smith, P.L. and Baenziger, J.U. 1992. Molecular basis of recognition by the glycoprotein hormone-specific N-acetylgalactosamine-transferase. Proc. Natl. Acad. Sci. USA 89:329-333.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 329-333
    • Smith, P.L.1    Baenziger, J.U.2
  • 62
  • 63
    • 0027099775 scopus 로고
    • Biosynthesis of sulfated glyco-protein-N-glycans present in recombinant human tissue plasminogen activator
    • Pfeiffer, G., Strube, K.H., and Geyer, R. 1992. Biosynthesis of sulfated glyco-protein-N-glycans present in recombinant human tissue plasminogen activator. Biochem. Biophys. Res. Commun. 189:1681-1685.
    • (1992) Biochem. Biophys. Res. Commun. , vol.189 , pp. 1681-1685
    • Pfeiffer, G.1    Strube, K.H.2    Geyer, R.3
  • 64
    • 0029161624 scopus 로고
    • Glycosylated human recombinant interleukin-1-α, neo interleukin-1-α, with d-mannose dimer exhibits selective activities in-vivo
    • Takei, Y., Chiba, T., Wada, K., Hayashi, H., Yamada, M., Kuwashima, J., et al. 1995. Glycosylated human recombinant interleukin-1-α, neo interleukin-1-α, with d-mannose dimer exhibits selective activities in-vivo. J. Interferon & Cytokine Res. 15:713-719.
    • (1995) J. Interferon & Cytokine Res. , vol.15 , pp. 713-719
    • Takei, Y.1    Chiba, T.2    Wada, K.3    Hayashi, H.4    Yamada, M.5    Kuwashima, J.6
  • 66
    • 0027944498 scopus 로고
    • The major form of the murine asialoglyco-protein receptor—cDNA sequence and expression in liver, testis and epididymis
    • Monroe, R.S. and Huber, B.E. 1994. The major form of the murine asialoglyco-protein receptor—cDNA sequence and expression in liver, testis and epididymis. Gene 148:237-244.
    • (1994) Gene , vol.148 , pp. 237-244
    • Monroe, R.S.1    Huber, B.E.2
  • 67
    • 0026557394 scopus 로고
    • Glycosylation of interleukin-6 purified from normal human blood mono-nuclear-cells
    • Parekh, R.B., Dwek, R.A., Rademacher, T.W., Opdenakker, G., and Vandamme, J. 1992. Glycosylation of interleukin-6 purified from normal human blood mono-nuclear-cells. Eur. J. Biochem. 203:135-141.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 135-141
    • Parekh, R.B.1    Dwek, R.A.2    Rademacher, T.W.3    Opdenakker, G.4    Vandamme, J.5
  • 68
    • 0026342559 scopus 로고
    • Clearing up glycoprotein hormones
    • Drickamer, K. 1991. Clearing up glycoprotein hormones. Cell 67:1029-1032.
    • (1991) Cell , vol.67 , pp. 1029-1032
    • Drickamer, K.1
  • 69
    • 0028891971 scopus 로고
    • Role of antennary structure of N-linked sugar chains in renal handling of recombinant human erythropoietin
    • Misaizu, T., Matsuki, S., Strickland, T.W., Takeuchi, M., Kobata, A., and Takasaki, S. 1995. Role of antennary structure of N-linked sugar chains in renal handling of recombinant human erythropoietin. Blood 86:4097-4104.
    • (1995) Blood , vol.86 , pp. 4097-4104
    • Misaizu, T.1    Matsuki, S.2    Strickland, T.W.3    Takeuchi, M.4    Kobata, A.5    Takasaki, S.6
  • 70
    • 0024366881 scopus 로고
    • Carbohydrate structures of human tissue plasminogen activator expressed in Chinese hamster ovary cells
    • Spellman, M.W., Basa, L.J., Leonard, C.K., Chakel, J.A., O’Connor, J.V., Wilson, S. et al. 1989. Carbohydrate structures of human tissue plasminogen activator expressed in Chinese hamster ovary cells. J. Biol. Chem. 264:14100-14111.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14100-14111
    • Spellman, M.W.1    Basa, L.J.2    Leonard, C.K.3    Chakel, J.A.4    O’Connor, J.V.5    Wilson, S.6
  • 71
    • 0023701160 scopus 로고
    • The influence of carbohydrate structure on the clearance of recombinant tissue-type plasminogen-activator
    • Hotchkiss, A., Refino, C.J., Leonard, C.K., Oconnor, J.V., Crowley, C., Mccabe, J., et al. 1988. The influence of carbohydrate structure on the clearance of recombinant tissue-type plasminogen-activator. Thromb. Haemost. 60:255-261.
    • (1988) Thromb. Haemost. , vol.60 , pp. 255-261
    • Hotchkiss, A.1    Refino, C.J.2    Leonard, C.K.3    Oconnor, J.V.4    Crowley, C.5    McCabe, J.6
  • 72
    • 0026641016 scopus 로고
    • Different culture methods lead to differences in glycosylation of a murine IgG monoclonal antibody
    • Patel, T.P., Parekh, R.B., Moellering, B.J., and Prior, C.P. 1992. Different culture methods lead to differences in glycosylation of a murine IgG monoclonal antibody. Biochem. J. 285:839-845.
    • (1992) Biochem. J. , vol.285 , pp. 839-845
    • Patel, T.P.1    Parekh, R.B.2    Moellering, B.J.3    Prior, C.P.4
  • 73
    • 0027460234 scopus 로고
    • Effect of culture conditions on IgM antibody structure, pharmacokinetics and activity
    • Maiorella, B.L., Winkelhake, J., Young, J., Moyer, B., Bauer, R., Hora, M., et al. 1993. Effect of culture conditions on IgM antibody structure, pharmacokinetics and activity. Bio/Technology 11:387-392.
    • (1993) Bio/Technology , vol.11 , pp. 387-392
    • Maiorella, B.L.1    Winkelhake, J.2    Young, J.3    Moyer, B.4    Bauer, R.5    Hora, M.6
  • 74
    • 0029097924 scopus 로고
    • Characterization of changes in the glycosylation pattern of recombinant proteins from BHK-21-cells due to different culture conditions
    • Gawlitzek, M., Valley, U., Nimtz, M., Wagner, R., and Conradt, H.S. 1995. Characterization of changes in the glycosylation pattern of recombinant proteins from BHK-21-cells due to different culture conditions. J. Biotechnol. 42:117-131.
    • (1995) J. Biotechnol. , vol.42 , pp. 117-131
    • Gawlitzek, M.1    Valley, U.2    Nimtz, M.3    Wagner, R.4    Conradt, H.S.5
  • 75
    • 0028721722 scopus 로고
    • Changes of monosaccharide availability of human hybridoma lead to alteration of biological properties of human monoclonal-antibody
    • Tachibana, H., Taniguchi, K., Ushio, Y., Teruya, K., Osada, K., and Murakami, H. 1994. Changes of monosaccharide availability of human hybridoma lead to alteration of biological properties of human monoclonal-antibody. Cytotechnology 16:151-157.
    • (1994) Cytotechnology , vol.16 , pp. 151-157
    • Tachibana, H.1    Taniguchi, K.2    Ushio, Y.3    Teruya, K.4    Osada, K.5    Murakami, H.6
  • 76
    • 84984774662 scopus 로고
    • The effect of dilution rate on CHO cell physiology and recombinant interferon-γ production in glucose-limited chemostat cultures
    • Hayter, P.M., Curling, E.M., Gould, M.L., Baines, A.J., Jenkins, N., Salmon, I., et al. 1993. The effect of dilution rate on CHO cell physiology and recombinant interferon-γ production in glucose-limited chemostat cultures. Biotechnol. Bioeng. 39:327-335.
    • (1993) Biotechnol. Bioeng. , vol.39 , pp. 327-335
    • Hayter, P.M.1    Curling, E.M.2    Gould, M.L.3    Baines, A.J.4    Jenkins, N.5    Salmon, I.6
  • 77
    • 0027112084 scopus 로고
    • Glucose-limited chemostat culture of Chinese hamster ovary cells producing recombinant human interferon-γ
    • Hayter, P.M., Curling, E.M., Baines, A.J., Jenkins, N., Salmon, I., Strange, P.G., et al. 1992. Glucose-limited chemostat culture of Chinese hamster ovary cells producing recombinant human interferon-γ. Biotechnol. Bioeng. 39:327-335.
    • (1992) Biotechnol. Bioeng. , vol.39 , pp. 327-335
    • Hayter, P.M.1    Curling, E.M.2    Baines, A.J.3    Jenkins, N.4    Salmon, I.5    Strange, P.G.6
  • 78
    • 0028896496 scopus 로고
    • The macroheterogeneity of recombinant human interferon-γ produced by Chinese hamster ovary cells is affected by the protein and lipid content of the culture medium
    • Castro, P.M.L., Ison, A.P., Hayter, P.M., and Bull, A.T. 1995. The macroheterogeneity of recombinant human interferon-γ produced by Chinese hamster ovary cells is affected by the protein and lipid content of the culture medium. Biotechnol. Appl. Biochem. 87:87-100.
    • (1995) Biotechnol. Appl. Biochem. , vol.87 , pp. 87-100
    • Castro, P.M.L.1    Ison, A.P.2    Hayter, P.M.3    Bull, A.T.4
  • 79
    • 0028706975 scopus 로고
    • Effect of lipid supplements on the production and glycosylation of recombinant interferon-γ expressed in CHO cells
    • Jenkins, N., Castro, P.M.L., Menon, S., Ison, A.P., and Bull, A.T. 1994. Effect of lipid supplements on the production and glycosylation of recombinant interferon-γ expressed in CHO cells. Cytotechnology 15:209-215.
    • (1994) Cytotechnology , vol.15 , pp. 209-215
    • Jenkins, N.1    Castro, P.M.L.2    Menon, S.3    Ison, A.P.4    Bull, A.T.5
  • 80
    • 0028909145 scopus 로고
    • The effect of increasing nucleotide sugar concentrations on the incorporation of sugars into glycoconjugates in rat hepatocytes
    • Rijcken, W.R.P., Overdijk, B., Vandeneijnden, D.H., and Ferwerda, W. 1995. The effect of increasing nucleotide sugar concentrations on the incorporation of sugars into glycoconjugates in rat hepatocytes. Biochem. J. 305:865-870.
    • (1995) Biochem. J. , vol.305 , pp. 865-870
    • Rijcken, W.R.P.1    Overdijk, B.2    Vandeneijnden, D.H.3    Ferwerda, W.4
  • 81
    • 0028765504 scopus 로고
    • Characterization of a recombinant antibody produced in the course of a high-yield fed-batch process
    • Robinson, D.K., Chan, C.P., Ip, C.Y., Tsai, P.K., Tung, J., Seamans, T.C., et al. 1994. Characterization of a recombinant antibody produced in the course of a high-yield fed-batch process. Biotechnol. Bioeng. 44:727-735.
    • (1994) Biotechnol. Bioeng. , vol.44 , pp. 727-735
    • Robinson, D.K.1    Chan, C.P.2    Ip, C.Y.3    Tsai, P.K.4    Tung, J.5    Seamans, T.C.6
  • 82
    • 0029411975 scopus 로고
    • N-glycans of recombinant human interferon-γ change during batch culture of chinese-hamster ovary cells
    • Hooker, A.D., Goldman, M.H., Markham, N.H., James, D.C., Ison, A.P., Bull, A.T., et al. 1995. N-glycans of recombinant human interferon-γ change during batch culture of chinese-hamster ovary cells. Biotechnol. Bioeng. 48:639-648.
    • (1995) Biotechnol. Bioeng. , vol.48 , pp. 639-648
    • Hooker, A.D.1    Goldman, M.H.2    Markham, N.H.3    James, D.C.4    Ison, A.P.5    Bull, A.T.6
  • 83
    • 0029014545 scopus 로고
    • Effect of different cell-culture conditions on the polypeptide integrity and N-glycosylation of a recombinant model glycoprotein
    • Gawlitzek, M., Conradt, H.S., and Wagner, R. 1995. Effect of different cell-culture conditions on the polypeptide integrity and N-glycosylation of a recombinant model glycoprotein. Biotechnol. Bioeng. 46:536-544.
    • (1995) Biotechnol. Bioeng. , vol.46 , pp. 536-544
    • Gawlitzek, M.1    Conradt, H.S.2    Wagner, R.3
  • 84
    • 0028707616 scopus 로고
    • The effect of protein-synthesis inhibitors on the glycosylation site occupancy of recombinant human prolactin
    • Shelikoff, M., Sinskey, A.J., and Stephanopoulos, G. 1994. The effect of protein-synthesis inhibitors on the glycosylation site occupancy of recombinant human prolactin. Cytotechnology 15:195-208.
    • (1994) Cytotechnology , vol.15 , pp. 195-208
    • Shelikoff, M.1    Sinskey, A.J.2    Stephanopoulos, G.3
  • 85
    • 0026688551 scopus 로고
    • Cell-free synthesis of enzymically active tissue-type plasminogen activator. Protein folding determines the extent of N-linked glycosylation
    • Bulleid, N.J., Bassel-Duby, R.S., Freedman, R.B., Sambrook, J.F., and Gething, M.J. 1992. Cell-free synthesis of enzymically active tissue-type plasminogen activator. Protein folding determines the extent of N-linked glycosylation. Biochem. J. 286:275-280.
    • (1992) Biochem. J. , vol.286 , pp. 275-280
    • Bulleid, N.J.1    Bassel-Duby, R.S.2    Freedman, R.B.3    Sambrook, J.F.4    Gething, M.J.5
  • 86
    • 0028946717 scopus 로고
    • Intracellular folding of tissue-type plasminogen-activator—effects of disulfide bond formation on N-linked glycosylation and secretion
    • Allen, S., Naim, H.Y., and Bulleid, N.J. 1995. Intracellular folding of tissue-type plasminogen-activator—effects of disulfide bond formation on N-linked glycosylation and secretion. J. Biol. Chem. 270:4797-4804.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4797-4804
    • Allen, S.1    Naim, H.Y.2    Bulleid, N.J.3
  • 87
    • 0027057767 scopus 로고
    • Growth-associated glycosylation of transferrin secreted by HepG2 cells
    • Hahn, T.J. and Goochee, C.F. 1992. Growth-associated glycosylation of transferrin secreted by HepG2 cells. J. Biol. Chem. 267:23982-23987.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23982-23987
    • Hahn, T.J.1    Goochee, C.F.2
  • 88
    • 0027457979 scopus 로고
    • Regulation of UDP-GlcNAc:Gal ß 1-3GalNAc-R ß 1-6-N-acetylglucosaminyltransferase (GlcNAc to GalNAc) in Chinese hamster ovary cells
    • Datti, A. and Dennis, J.W. 1993. Regulation of UDP-GlcNAc:Gal ß 1-3GalNAc-R ß 1-6-N-acetylglucosaminyltransferase (GlcNAc to GalNAc) in Chinese hamster ovary cells. J. Biol. Chem. 268:5409-5416.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5409-5416
    • Datti, A.1    Dennis, J.W.2
  • 89
    • 0028725582 scopus 로고
    • Role of environmental-conditions on the expression levels, glycoform pattern and levels of sialyltransferase for hFSH produced by recombinant CHO cells
    • Chotigeat, W., Watanapokasin, Y., Mahler, S., and Gray, P.P. 1994. Role of environmental-conditions on the expression levels, glycoform pattern and levels of sialyltransferase for hFSH produced by recombinant CHO cells. Cytotechnology 15:217-221.
    • (1994) Cytotechnology , vol.15 , pp. 217-221
    • Chotigeat, W.1    Watanapokasin, Y.2    Mahler, S.3    Gray, P.P.4
  • 90
    • 0028854693 scopus 로고
    • Expression of FSH in CHO cells .2. stimulation of hFSH expression levels by defined medium supplements
    • Gebert, C.A. and Gray, P.P. 1995. Expression of FSH in CHO cells .2. stimulation of hFSH expression levels by defined medium supplements. Cytotechnology 17:13-19.
    • (1995) Cytotechnology , vol.17 , pp. 13-19
    • Gebert, C.A.1    Gray, P.P.2
  • 91
    • 0026707317 scopus 로고
    • N-butyrate reduces the expression of ß-galactoside α2, 6-sialyltransferase in Hep G2 cells
    • Shah, S., Lance, P., Smith, T.J., Berenson, C.S., Cohen, S.A., Horvath, P.J., et al. 1992. N-butyrate reduces the expression of ß-galactoside α2, 6-sialyltransferase in Hep G2 cells. J. Biol. Chem. 267:10652-10658.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10652-10658
    • Shah, S.1    Lance, P.2    Smith, T.J.3    Berenson, C.S.4    Cohen, S.A.5    Horvath, P.J.6
  • 92
    • 0027626501 scopus 로고
    • Production of tPA in recombinant CHO cells under oxygen-limited conditions
    • Lin, A.A., Kimura, R., and Miller, W.M. 1993. Production of tPA in recombinant CHO cells under oxygen-limited conditions. Biotechnol. Bioeng. 42:339-350.
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 339-350
    • Lin, A.A.1    Kimura, R.2    Miller, W.M.3
  • 93
    • 14744285958 scopus 로고
    • Culture pH affects expression rates and glycosylation of recombinant mouse placental lactogen proteins by chinese hamster ovary (CHO) cells
    • Borys, M.C., Linzer, D.J.H., and Papoutsakis, E.T. 1993. Culture pH affects expression rates and glycosylation of recombinant mouse placental lactogen proteins by chinese hamster ovary (CHO) cells. Bio/Technology 11:720-724.
    • (1993) Bio/Technology , vol.11 , pp. 720-724
    • Borys, M.C.1    Linzer, D.J.H.2    Papoutsakis, E.T.3
  • 94
    • 0027957068 scopus 로고
    • Monosaccharide and oligosaccharide analysis of isoelectric focusing-separated and blotted granulocyte-colony-stimulating factor glycoforms using high-pH anion-exchange chromatography with pulsed amperometric detection
    • Andersen, D.C., Goochee, C.F., Cooper, G., and Weitzhandler, M. 1994. Monosaccharide and oligosaccharide analysis of isoelectric focusing-separated and blotted granulocyte-colony-stimulating factor glycoforms using high-pH anion-exchange chromatography with pulsed amperometric detection. Glycobiology 4:459-467.
    • (1994) Glycobiology , vol.4 , pp. 459-467
    • Andersen, D.C.1    Goochee, C.F.2    Cooper, G.3    Weitzhandler, M.4
  • 95
    • 0028393399 scopus 로고
    • Ammonia affects the glycosylation patterns of recombinant mouse placental lactogen-1 by chinese-hamster ovary cells in a pH-dependent manner
    • Borys, M.C., Linzer, D.I.H., and Papoutsakis, E.T. 1994. Ammonia affects the glycosylation patterns of recombinant mouse placental lactogen-1 by chinese-hamster ovary cells in a pH-dependent manner. Biotechnol. Bioeng. 43:505-514.
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 505-514
    • Borys, M.C.1    Linzer, D.I.H.2    Papoutsakis, E.T.3
  • 96
    • 0027628305 scopus 로고
    • Glycosidase activities in chinese-hamster ovary cell lysate and cell-culture supernatant
    • Gramer, M.J. and Goochee, C.F. 1993. Glycosidase activities 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
  • 97
    • 0029053768 scopus 로고
    • Removal of sialic acid from a glycoprotein in CHO cell supernatant by action of an extracellular CHO cell sialidase
    • Gramer, M.J., Goochee, C.F., Chock, V., Brousseau, D.T., and Sliwkowski, M.B. 1995. Removal of sialic acid from a glycoprotein in CHO cell 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    Chock, V.3    Brousseau, D.T.4    Sliwkowski, M.B.5
  • 98
    • 0027495339 scopus 로고
    • Isolation and properties of a soluble sialidase from the culture fluid of chinese-hamster ovary cells
    • Warner, T.G., Chang, J., Ferrari, J., Harris, R., Mcnerney, T., Bennett, G., et al. 1993. Isolation and properties of a soluble sialidase from the culture fluid of chinese-hamster ovary cells. Glycobiology 3:455-463.
    • (1993) Glycobiology , vol.3 , pp. 455-463
    • Warner, T.G.1    Chang, J.2    Ferrari, J.3    Harris, R.4    McNerney, T.5    Bennett, G.6
  • 99
    • 0028283168 scopus 로고
    • Cloning and expression of a soluble sialidase from chinese-hamster ovary cells—sequence alignment similarities to bacterial sialidases
    • Ferrari, J., Harris, R., and Warner, T.G. 1994. Cloning and expression of a soluble sialidase from chinese-hamster ovary cells—sequence alignment similarities to bacterial sialidases. Glycobiology 4:367-373.
    • (1994) Glycobiology , vol.4 , pp. 367-373
    • Ferrari, J.1    Harris, R.2    Warner, T.G.3
  • 100
    • 0028172722 scopus 로고
    • Purification and characterization of α-l-fucosidase from chinese-hamster ovary cell-culture supernatant
    • Gramer, M.J., Schaffer, D.V., Sliwkowski, M.B., and Goochee, C.F. 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.B.3    Goochee, C.F.4
  • 101
    • 0028166666 scopus 로고
    • Glycosidase activities of the 293 and NS0 cell-lines, and of an antibody-producing hybridoma cell-line
    • Gramer, M.J. and Goochee, C.F. 1994. Glycosidase activities of the 293 and NS0 cell-lines, and of an antibody-producing hybridoma cell-line. Biotechnol. Bioeng. 43:423-428.
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 423-428
    • Gramer, M.J.1    Goochee, C.F.2
  • 102
    • 0028800666 scopus 로고
    • Influence of cell-derived and media-derived factors on the integrity of a human monoclonal-antibody after secretion into serum-free cell-culture supernatants
    • Ackermann, M., Marx, U., and Jager, V. 1995. Influence of cell-derived and media-derived factors on the integrity of a human monoclonal-antibody after secretion into serum-free cell-culture supernatants. Biotechnol. Bioeng. 45:97-106.
    • (1995) Biotechnol. Bioeng. , vol.45 , pp. 97-106
    • Ackermann, M.1    Marx, U.2    Jager, V.3
  • 103
    • 0028803048 scopus 로고
    • Synthesis of a glycopeptide carrying a N-linked core pentasaccharide
    • Matsuo, I., Nakahara, Y., Ito, Y., Nukada, T., and Ogawa, T. 1995. Synthesis of a glycopeptide carrying a N-linked core pentasaccharide. Bio-organic & Med. Chem. 3:1455-1463.
    • (1995) Bio-Organic & Med. Chem. , vol.3 , pp. 1455-1463
    • Matsuo, I.1    Nakahara, Y.2    Ito, Y.3    Nukada, T.4    Ogawa, T.5
  • 104
    • 0030050797 scopus 로고    scopus 로고
    • Rationally designed syntheses of high-mannose and complex type undecasaocharides
    • Nakahara, Y., Shibayama, S., and Ogawa, T. 1996. Rationally designed syntheses of high-mannose and complex type undecasaocharides. Carbohyd. Res. 280:67-84.
    • (1996) Carbohyd. Res. , vol.280 , pp. 67-84
    • Nakahara, Y.1    Shibayama, S.2    Ogawa, T.3
  • 105
    • 0027158301 scopus 로고
    • A new multienzyme system for a one-pot synthesis of sialyl oligosaccharides—combined use of ß-galactosidase and α(2, 6)-sialyltransferase coupled with regeneration in situ of CMP-sialic acid
    • Herrmann, G.F., Ichikawa, Y., Wandrey, C., Gaeta, F.C.A., Paulson, J.C., and Wong, C.H. 1993. A new multienzyme system for a one-pot synthesis of sialyl oligosaccharides—combined use of ß-galactosidase and α(2, 6)-sialyltransferase coupled with regeneration in situ of CMP-sialic acid. Tetrahedron Lett. 34:3091-3094.
    • (1993) Tetrahedron Lett , vol.34 , pp. 3091-3094
    • Herrmann, G.F.1    Ichikawa, Y.2    Wandrey, C.3    Gaeta, F.C.A.4    Paulson, J.C.5    Wong, C.H.6
  • 106
    • 0029417268 scopus 로고
    • α-galactosyl (Ga1-α-1-3Gal-ß-1-4GlcNAc-r) epitopes on human-cells—synthesis of the epitope on human red-cells by recombinant primate α1, 3-galactosyltransferase expressed in Escherichia coli
    • Galili, U. and Anaraki, F. 1995. α-galactosyl (Ga1-α-1-3Gal-ß-1-4GlcNAc-r) epitopes on human-cells—synthesis of the epitope on human red-cells by recombinant primate α1, 3-galactosyltransferase expressed in Escherichia coli. Glycobiology 5:775-782.
    • (1995) Glycobiology , vol.5 , pp. 775-782
    • Galili, U.1    Anaraki, F.2


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