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Volumn 100, Issue 4, 2008, Pages 721-733

Influence of intracellular nucleotide and nucleotide sugar contents on recombinant interferon-γ glycosylation during batch and fed-batch cultures of CHO cells

Author keywords

CHO cells; Energetic status; Glycosylation macroheterogeneity; IFN 7; Nucleotide sugars

Indexed keywords

BATCH CELL CULTURE; BATCH DATA PROCESSING; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; CELLS; ESTERIFICATION; GLYCOSYLATION; INTERNET PROTOCOLS; NUCLEIC ACIDS; NUCLEOTIDES; SUGAR (SUCROSE); SUGARS; SYNTHESIS (CHEMICAL);

EID: 46249121065     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.21816     Document Type: Article
Times cited : (46)

References (55)
  • 1
    • 0028946717 scopus 로고
    • Intracellular folding of tissue-type plasminogen activator
    • Allen S, Naim HY, Bulleid NJ. 1995. Intracellular folding of tissue-type plasminogen activator. 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
  • 2
    • 0029636676 scopus 로고
    • The effect of ammonia on the O-linked glycosylation of granulocyte colony-stimulating factor produced by Chinese hamster ovary cells
    • Andersen DC, Goochee CF. 1995. The effect of ammonia on the O-linked glycosylation of granulocyte colony-stimulating factor produced by Chinese hamster ovary cells. Biotechnol Bioeng 47:96-105.
    • (1995) Biotechnol Bioeng , vol.47 , pp. 96-105
    • Andersen, D.C.1    Goochee, C.F.2
  • 4
    • 0033751654 scopus 로고    scopus 로고
    • The effect of glucose and glutamine on the intracellular nucleotide pool and oxygen uptake rate of a murine hybridoma
    • Barnabé N, Butler M. 2000. The effect of glucose and glutamine on the intracellular nucleotide pool and oxygen uptake rate of a murine hybridoma. Cytotechnology 34:47-57.
    • (2000) Cytotechnology , vol.34 , pp. 47-57
    • Barnabé, N.1    Butler, M.2
  • 5
    • 14744285958 scopus 로고
    • Culture pH affects expression rates and glycosylation of recombinant mouse placental lactogen proteins by 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 by Chinese hamster ovary (CHO) cells. Biotechnology 11: 720-724.
    • (1993) Biotechnology , vol.11 , pp. 720-724
    • Borys, M.C.1    Linzer, D.I.2    Papoutsakis, E.T.3
  • 6
    • 0028393399 scopus 로고
    • Ammonia affects the glycosylation patterns of recombinant mouse placental lactogen-I by Chinese hamster ovary cells in a pH-dependant manner
    • Borys MC, Linzer DI, Papoutsakis ET. 1994. Ammonia affects the glycosylation patterns of recombinant mouse placental lactogen-I by Chinese hamster ovary cells in a pH-dependant manner. Biotechnol Bioeng 43:505-514.
    • (1994) Biotechnol Bioeng , vol.43 , pp. 505-514
    • Borys, M.C.1    Linzer, D.I.2    Papoutsakis, E.T.3
  • 8
    • 23844433927 scopus 로고    scopus 로고
    • Animal cell cultures: Recent achievements and perspectives in the production of biopharmaceuticals
    • Butler M. 2005. Animal cell cultures: Recent achievements and perspectives in the production of biopharmaceuticals. Appl Microb Biotechnol 68:283-291.
    • (2005) Appl Microb Biotechnol , vol.68 , pp. 283-291
    • Butler, M.1
  • 9
    • 0028896496 scopus 로고
    • The macroheterogeneity of recombinant human interferon-gamma produced by Chinese-hamster ovary cells is affected by the protein and lipid content of the culture medium
    • Castro PML, Ison AP, Hayter PM, Bull AT. 1995. The macroheterogeneity of recombinant human interferon-gamma produced by Chinese-hamster ovary cells is affected by the protein and lipid content of the culture medium. Biotechnol Appl Biochem 21:87-100.
    • (1995) Biotechnol Appl Biochem , vol.21 , pp. 87-100
    • Castro, P.M.L.1    Ison, A.P.2    Hayter, P.M.3    Bull, A.T.4
  • 10
    • 0033589362 scopus 로고    scopus 로고
    • Cell lines with reduced UDP-N-acetylhexosamine pool in the presence of ammonium
    • Cayli A, Hirschmann F, Wirt M, Hauser H. 1999. Cell lines with reduced UDP-N-acetylhexosamine pool in the presence of ammonium. Biotechnol Bioeng 65:192-200.
    • (1999) Biotechnol Bioeng , vol.65 , pp. 192-200
    • Cayli, A.1    Hirschmann, F.2    Wirt, M.3    Hauser, H.4
  • 11
    • 19544383966 scopus 로고    scopus 로고
    • Gene-expression profiles for five key glycosylation genes for galactose-fed CHO cells expressing recombinant IL-4/13 cytokine trap
    • Clark KJR, Griffiths J, Bailey KM, Harcum SW. 2005. Gene-expression profiles for five key glycosylation genes for galactose-fed CHO cells expressing recombinant IL-4/13 cytokine trap. Biotechnol Bioeng 90: 568-577.
    • (2005) Biotechnol Bioeng , vol.90 , pp. 568-577
    • Clark, K.J.R.1    Griffiths, J.2    Bailey, K.M.3    Harcum, S.W.4
  • 12
    • 0025649375 scopus 로고
    • Recombinant human interferon-γ. Differences in glycosylation and proteolytic processing lead to heterogeneity in batch culture
    • Curling EMA, Hayter PM, Baines AJ, Bull AT, Gull K, Strange PG, Jenkins N. 1990. Recombinant human interferon-γ. Differences in glycosylation and proteolytic processing lead to heterogeneity in batch culture. Biochem J 272:333-337.
    • (1990) Biochem J , vol.272 , pp. 333-337
    • Curling, E.M.A.1    Hayter, P.M.2    Baines, A.J.3    Bull, A.T.4    Gull, K.5    Strange, P.G.6    Jenkins, N.7
  • 13
    • 0029636508 scopus 로고
    • Fluorophore-labeled glycan analysis of immunoglobulin fusion proteins: Correlation of oligosaccharide content with in vivo clearance rate profile
    • Flesher ER, Marzowski K, Wang WC, Raff HV. 1995. Fluorophore-labeled glycan analysis of immunoglobulin fusion proteins: Correlation of oligosaccharide content with in vivo clearance rate profile. Biotechnol Bioeng 46:399-407.
    • (1995) Biotechnol Bioeng , vol.46 , pp. 399-407
    • Flesher, E.R.1    Marzowski, K.2    Wang, W.C.3    Raff, H.V.4
  • 14
    • 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, Conradt HS. 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
  • 15
    • 0032485239 scopus 로고    scopus 로고
    • Ammonium ion and glucosamine dependent increases of oligosaccharide complexity in recombinant glycoproteins secreted from cultivated BHK-21 cells
    • Gawlitzek M, Valley U, Wagner R. 1998. Ammonium ion and glucosamine dependent increases of 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
  • 16
    • 8344271025 scopus 로고    scopus 로고
    • Advances in the production of human therapeutic proteins in yeasts and filamentous fungi
    • Gerngross TU. 2004. Advances in the production of human therapeutic proteins in yeasts and filamentous fungi. Nat Biotechnol 22:1409-1414.
    • (2004) Nat Biotechnol , vol.22 , pp. 1409-1414
    • Gerngross, T.U.1
  • 17
    • 0032488375 scopus 로고    scopus 로고
    • Monitoring recombinant human interferon-gamma N-glycosylation during perfused fluidized-bed and stirred-tank batch culture of CHO cells
    • Goldman MH, James DC, Rendall M, Ison AP, Hoare M, Bull AT. 1998. Monitoring recombinant human interferon-gamma 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.P.4    Hoare, M.5    Bull, A.T.6
  • 18
    • 0032078486 scopus 로고    scopus 로고
    • Intracellular UDP-N-Acetylhexosamine pool affects N-glycan complexity: A mechanism of ammonium action on protein glycosylation
    • Grammatikos SI, Valley U, Nimtz M, Conradt HS, Wagner R. 1998. Intracellular UDP-N-Acetylhexosamine pool affects N-glycan complexity: A mechanism of ammonium action on protein glycosylation. Biotechnol Prog 14:410-419.
    • (1998) Biotechnol Prog , vol.14 , pp. 410-419
    • Grammatikos, S.I.1    Valley, U.2    Nimtz, M.3    Conradt, H.S.4    Wagner, R.5
  • 21
    • 0027910076 scopus 로고
    • The effect of the dilution rate on CHO cell physiology and recombinant interferon-γ production in glucose-limited chemostat culture
    • Hayter PM, Curling EMA, Gould ML, Baines AJ, Jenkins N, Salmon IPG, Bull AT. 1993. The effect of the dilution rate on CHO cell physiology and recombinant interferon-γ production in glucose-limited chemostat culture. Biotechnol Bioeng 42:1077-1085.
    • (1993) Biotechnol Bioeng , vol.42 , pp. 1077-1085
    • Hayter, P.M.1    Curling, E.M.A.2    Gould, M.L.3    Baines, A.J.4    Jenkins, N.5    Salmon, I.P.G.6    Bull, A.T.7
  • 22
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • Helenius A. 1994. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol Biol Cell 5:253-265.
    • (1994) Mol Biol Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 23
    • 0035922885 scopus 로고    scopus 로고
    • Metabolic control of recombinant monoclonal antibody N-glycosylation in GS-NS0 cells
    • Hills AE, Patel A, Boyd P, James DC. 2001. Metabolic control of recombinant monoclonal antibody N-glycosylation in GS-NS0 cells. Biotechnol Bioeng 75:239-251.
    • (2001) Biotechnol Bioeng , vol.75 , pp. 239-251
    • Hills, A.E.1    Patel, A.2    Boyd, P.3    James, D.C.4
  • 24
    • 0029953675 scopus 로고    scopus 로고
    • Competition between folding and glycosylation in the endoplasmic reticulum
    • Hoist B, Bruun AW, Kielland-Brandt MC, Winther JR. 1996. Competition between folding and glycosylation in the endoplasmic reticulum. EMBO J 15:3538-3546.
    • (1996) EMBO J , vol.15 , pp. 3538-3546
    • Hoist, B.1    Bruun, A.W.2    Kielland-Brandt, M.C.3    Winther, J.R.4
  • 25
    • 0028224656 scopus 로고
    • Glycosylation of recombinant proteins: Problems and prospects
    • Jenkins N, Curling EMA. 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.A.2
  • 26
    • 0028706975 scopus 로고
    • Effect of lipid supplements on the production and glycosylation of recombinant interferon-γ expressed in CHO cells
    • Jenkins N, Castro PMI, Menon S, Ison AP, Bull AT. 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.I.2    Menon, S.3    Ison, A.P.4    Bull, A.T.5
  • 27
    • 46249088222 scopus 로고    scopus 로고
    • Getting the glycosylation right: Implications for the industry
    • Jenkins N, Parekh RB, James DC. 1996. Getting the glycosylation right: Implications for the industry. Nat Biotechnol 14:315-322.
    • (1996) Nat Biotechnol , vol.14 , pp. 315-322
    • Jenkins, N.1    Parekh, R.B.2    James, D.C.3
  • 28
    • 29244453502 scopus 로고    scopus 로고
    • Intracellular nucleotides and nucleotide sugars content of cultured CHO cells determined by a fast, sensitive and high resolution ion-pair RP-HPLC
    • Kochanowski N, Blanchard F, Cacan R, Chirat F, Guedon E, Marc A, Goergen JL. 2006. Intracellular nucleotides and nucleotide sugars content of cultured CHO cells determined by a fast, sensitive and high resolution ion-pair RP-HPLC. Anal Biochem 348:243-251.
    • (2006) Anal Biochem , vol.348 , pp. 243-251
    • Kochanowski, N.1    Blanchard, F.2    Cacan, R.3    Chirat, F.4    Guedon, E.5    Marc, A.6    Goergen, J.L.7
  • 29
    • 0031831143 scopus 로고    scopus 로고
    • Carbohydrate-deficient glycoprotein syndrome type 1: Correction of the glycosylation defect by deprivation of glucose or supplementation of mannose
    • Kömer C, Lehle L, Von Figura K. 1998. Carbohydrate-deficient glycoprotein syndrome type 1: Correction of the glycosylation defect by deprivation of glucose or supplementation of mannose. Glycoconj J 15:499-505.
    • (1998) Glycoconj J , vol.15 , pp. 499-505
    • Kömer, C.1    Lehle, L.2    Von Figura, K.3
  • 30
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld R, Kornfeld S. 1985. Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 54:631-634.
    • (1985) Annu Rev Biochem , vol.54 , pp. 631-634
    • Kornfeld, R.1    Kornfeld, S.2
  • 32
    • 0032916777 scopus 로고    scopus 로고
    • Na-butyrate increases the production and α2,6-sialylation of recombinant interferon-γ expressed by α2,6-sialyltransferase engineered CHO cells
    • Lamotte D, Buckberry L, Monaco L, Soria M, Jenkins N, Engasser JM, Marc A. 1999. Na-butyrate increases the production and α2,6-sialylation of recombinant interferon-γ expressed by α2,6-sialyltransferase engineered CHO cells. Cytotechnology 29:55-64.
    • (1999) Cytotechnology , vol.29 , pp. 55-64
    • Lamotte, D.1    Buckberry, L.2    Monaco, L.3    Soria, M.4    Jenkins, N.5    Engasser, J.M.6    Marc, A.7
  • 33
    • 0031239859 scopus 로고    scopus 로고
    • Effects of ammonium and lactate on growth and metabolism of a recombinant CHO cell culture
    • Lao M-S, Toth D. 1997. Effects of ammonium and lactate on growth and metabolism of a recombinant CHO cell culture. Biotechnol Prog 13: 688-691.
    • (1997) Biotechnol Prog , vol.13 , pp. 688-691
    • Lao, M.-S.1    Toth, D.2
  • 34
    • 34250092706 scopus 로고
    • Transient responses of hybri-doma cells to lactate and ammonia pulse and steps changes in continuous culture
    • Miller WM, Wilke CR, Blanch HW. 1988. Transient responses of hybri-doma cells to lactate and ammonia pulse and steps changes in continuous culture. Bioproc Eng 3:113-122.
    • (1988) Bioproc Eng , vol.3 , pp. 113-122
    • Miller, W.M.1    Wilke, C.R.2    Blanch, H.W.3
  • 35
    • 1042265424 scopus 로고    scopus 로고
    • Fortification of a protein-free cell culture medium with plant peptones improves cultivation and productivity of an interferon-γ producing CHO cell line
    • Mols J, Burteau CC, Verhoeye FR, Ballez JS, Agathos SN, Schneider YJ. 2003. Fortification of a protein-free cell culture medium with plant peptones improves cultivation and productivity of an interferon-γ producing CHO cell line. In Vitro Cell Dev Biol Anim 39:291-296.
    • (2003) In Vitro Cell Dev Biol Anim , vol.39 , pp. 291-296
    • Mols, J.1    Burteau, C.C.2    Verhoeye, F.R.3    Ballez, J.S.4    Agathos, S.N.5    Schneider, Y.J.6
  • 36
    • 0028518583 scopus 로고
    • An in vitro approach for the expression of recombinant proteins in mammalian cells
    • Monaco L, Tagliabue R, Soria MR, Uhlen M. 1994. An in vitro approach for the expression of recombinant proteins in mammalian cells. Biotechnol Appl Biochem 20:157-171.
    • (1994) Biotechnol Appl Biochem , vol.20 , pp. 157-171
    • Monaco, L.1    Tagliabue, R.2    Soria, M.R.3    Uhlen, M.4
  • 37
    • 0030425381 scopus 로고    scopus 로고
    • Genetic engineering of alpha2,6-sialyltransferase in recombinant CHO cells and its effect on the sialylation of recombinant interferon-γ
    • Monaco L, Marc A, Eon-Duval A, Acerbis G, Distefano G, Lamotte D, Engasser JM, Soria M, Jenkins N. 1996. Genetic engineering of alpha2,6-sialyltransferase in recombinant CHO cells and its effect on the sialylation of recombinant interferon-γ. Cytotechnology 22:197-203.
    • (1996) Cytotechnology , vol.22 , pp. 197-203
    • Monaco, L.1    Marc, A.2    Eon-Duval, A.3    Acerbis, G.4    Distefano, G.5    Lamotte, D.6    Engasser, J.M.7    Soria, M.8    Jenkins, N.9
  • 39
    • 0033524678 scopus 로고    scopus 로고
    • Metabolic effects on recombinant interferon-γ glycosylation in continuous culture of Chinese hamster ovary cells
    • Nyberg GB, Balcarcel RR, Follstad BD, Stephanopoulos G, Wang DIC. 1999. Metabolic effects on recombinant interferon-γ glycosylation in continuous culture of Chinese hamster ovary cells. Biotechnol Bioeng 62:336-347.
    • (1999) Biotechnol Bioeng , vol.62 , pp. 336-347
    • Nyberg, G.B.1    Balcarcel, R.R.2    Follstad, B.D.3    Stephanopoulos, G.4    Wang, D.I.C.5
  • 40
    • 0032890448 scopus 로고    scopus 로고
    • Chinese hamster ovary cells with reduced hexokinase activity maintain normal GDP-Mannose levels
    • O'Rear JL, Scocca JR, Walker BK, Krag SS. 1999. Chinese hamster ovary cells with reduced hexokinase activity maintain normal GDP-Mannose levels. J Cell Biochem 72:56-66.
    • (1999) J Cell Biochem , vol.72 , pp. 56-66
    • O'Rear, J.L.1    Scocca, J.R.2    Walker, B.K.3    Krag, S.S.4
  • 41
    • 0026235117 scopus 로고
    • Mammalian cell gene expression: Protein glycosylation
    • Parekh RB. 1991. Mammalian cell gene expression: Protein glycosylation. Curr Opin Biotechnol 2:730-734.
    • (1991) Curr Opin Biotechnol , vol.2 , pp. 730-734
    • Parekh, R.B.1
  • 42
  • 43
    • 0028909145 scopus 로고
    • The effect of increasing nucleotide sugar concentrations on the incorporation of sugars into glyconjugates in rat hepatocytes
    • Pels Rijcken WRP, Overdijck B, Vandneijnden DH, Ferwerda W. 1995. The effect of increasing nucleotide sugar concentrations on the incorporation of sugars into glyconjugates in rat hepatocytes. Biochem J 305:865-870.
    • (1995) Biochem J , vol.305 , pp. 865-870
    • Pels Rijcken, W.R.P.1    Overdijck, B.2    Vandneijnden, D.H.3    Ferwerda, W.4
  • 44
    • 0026737392 scopus 로고
    • Intracellular ribonucleotide pools as a tool for monitoring the physiological state of in vitro cultivated mammalian cells during production processes
    • Ryll T, Wagner R. 1992. Intracellular ribonucleotide pools as a tool for monitoring the physiological state of in vitro cultivated mammalian cells during production processes. Biotechnol Bioeng 40:934-946.
    • (1992) Biotechnol Bioeng , vol.40 , pp. 934-946
    • Ryll, T.1    Wagner, R.2
  • 45
    • 0028452886 scopus 로고
    • Biochemistry of growth inhibition by ammonium ions in mammalian cells
    • Ryll T, Valley U, Wagner R. 1994. Biochemistry of growth inhibition by ammonium ions in mammalian cells. Biotechnol Bioeng 44:184-193.
    • (1994) Biotechnol Bioeng , vol.44 , pp. 184-193
    • Ryll, T.1    Valley, U.2    Wagner, R.3
  • 46
    • 0028052164 scopus 로고
    • Role of N-glycosylation in the synthesis, dimerization and secretion of human interferon-gamma
    • Sareneva T, Pirhonen J, Cantell K, Kalkkinen N, Julkunen I. 1994. Role of N-glycosylation in the synthesis, dimerization and secretion of human interferon-gamma. Biochem J 303:831-840.
    • (1994) Biochem J , vol.303 , pp. 831-840
    • Sareneva, T.1    Pirhonen, J.2    Cantell, K.3    Kalkkinen, N.4    Julkunen, I.5
  • 47
    • 1042283686 scopus 로고
    • Optimization of hybridoma cell growth and monoclonal antibody secretion in chemically defined serum- and protein-free medium
    • Schneider YJ. 1989. Optimization of hybridoma cell growth and monoclonal antibody secretion in chemically defined serum- and protein-free medium. J Immunol Methods 116:67-77.
    • (1989) J Immunol Methods , vol.116 , pp. 67-77
    • Schneider, Y.J.1
  • 49
    • 0035043099 scopus 로고    scopus 로고
    • Assay for hexosamine pathway intermediates (uridine dipho-sphate-N-acetyl amino sugars) in small samples of human muscle tissue
    • Span PN, Pouwels MJ, Olthaar AJ, Bosch RR, Hermus RMM, Sweep CGJ. 2001. Assay for hexosamine pathway intermediates (uridine dipho-sphate-N-acetyl amino sugars) in small samples of human muscle tissue. Tech Briefs 47:944-946.
    • (2001) Tech Briefs , vol.47 , pp. 944-946
    • Span, P.N.1    Pouwels, M.J.2    Olthaar, A.J.3    Bosch, R.R.4    Hermus, R.M.M.5    Sweep, C.G.J.6
  • 50
    • 0027170427 scopus 로고
    • La glycosylation des protéines recombinantes.
    • Verbert A. 1993. La glycosylation des protéines recombinantes. Biofutur 125:40-43.
    • (1993) Biofutur , vol.125 , pp. 40-43
    • Verbert, A.1
  • 51
    • 33746163862 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks 2006
    • Walsh G. 2006. Biopharmaceutical benchmarks 2006. Nat Biotechnol 24:769-776.
    • (2006) Nat Biotechnol , vol.24 , pp. 769-776
    • Walsh, G.1
  • 52
    • 12544253860 scopus 로고    scopus 로고
    • Impact of dynamic online fed-batch strategies on metabolism, productivity and N- glycosylation quality in CHO cell cultures
    • Wong DCF, Wong KTK, Goh LT, Heng CK, Yap MGS. 2004. Impact of dynamic online fed-batch strategies on metabolism, productivity and N- glycosylation quality in CHO cell cultures. Biotechnol Bioeng 89: 164-177.
    • (2004) Biotechnol Bioeng , vol.89 , pp. 164-177
    • Wong, D.C.F.1    Wong, K.T.K.2    Goh, L.T.3    Heng, C.K.4    Yap, M.G.S.5
  • 53
    • 0030220095 scopus 로고    scopus 로고
    • The structural role of sugars in glycoproteins
    • Wyss DF, Wagner G. 1996. The structural role of sugars in glycoproteins. Curr Opin Biotechnol 7:409-416.
    • (1996) Curr Opin Biotechnol , vol.7 , pp. 409-416
    • Wyss, D.F.1    Wagner, G.2
  • 54
    • 0031555512 scopus 로고    scopus 로고
    • Gamma-IFN production and quality in stochiometric fed-batch cultures of CHO cells under serum-free conditions
    • Xie L, Nyberg G, Gu X, Li H, Möllborn F, Wang DIC. 1997. Gamma-IFN production and quality in stochiometric fed-batch cultures of CHO cells under serum-free conditions. Biotechnol Bioeng 56:577-582.
    • (1997) Biotechnol Bioeng , vol.56 , pp. 577-582
    • Xie, L.1    Nyberg, G.2    Gu, X.3    Li, H.4    Möllborn, F.5    Wang, D.I.C.6
  • 55
    • 0036793115 scopus 로고    scopus 로고
    • Glycosylation by Chinese hamster ovary cells in dolichol phosphate-supplemented cultures
    • Yuk IHY, Wang DIC. 2002. Glycosylation by Chinese hamster ovary cells in dolichol phosphate-supplemented cultures. Biotechnol Appl Biochem 36:141-147.
    • (2002) Biotechnol Appl Biochem , vol.36 , pp. 141-147
    • Yuk, I.H.Y.1    Wang, D.I.C.2


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