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Volumn 386, Issue 2, 2009, Pages 228-236

Mass spectrometric quantification of neutral and sialylated N-glycans from a recombinant therapeutic glycoprotein produced in the two Chinese hamster ovary cell lines

Author keywords

CHO cell; Girard's reagent T; MALDI TOF; Methyl esterification; Quantification; Sialylated glycan

Indexed keywords

BIOACTIVITY; CELL CULTURE; CELLS; ESTERS; GLYCOPROTEINS; INDUCTIVELY COUPLED PLASMA; MASS SPECTROMETRY; OLIGOSACCHARIDES; QUALITY CONTROL; REAGENTS;

EID: 59749083362     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.12.015     Document Type: Article
Times cited : (28)

References (30)
  • 1
    • 0033038265 scopus 로고    scopus 로고
    • Genetic optimization of recombinant glycoprotein production by mammalian cells
    • Fussenegger M., Bailey J.E., Hauser H., and Mueller P.P. Genetic optimization of recombinant glycoprotein production by mammalian cells. Trends Biotechnol. 17 (1999) 35-42
    • (1999) Trends Biotechnol. , vol.17 , pp. 35-42
    • Fussenegger, M.1    Bailey, J.E.2    Hauser, H.3    Mueller, P.P.4
  • 2
    • 33746750608 scopus 로고    scopus 로고
    • Challenges in therapeutic glycoprotein production
    • Sethuraman N., and Stadheim T.A. Challenges in therapeutic glycoprotein production. Curr. Opin. Biotechnol. 17 (2006) 341-346
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 341-346
    • Sethuraman, N.1    Stadheim, T.A.2
  • 3
    • 21644488322 scopus 로고    scopus 로고
    • Production of therapeutic glycoproteins through the engineering of glycosylation pathway in yeast
    • Roy S.K., Chiba Y., and Jigami Y. Production of therapeutic glycoproteins through the engineering of glycosylation pathway in yeast. Biotechnol. Bioprocess Eng. 5 (2000) 219-226
    • (2000) Biotechnol. Bioprocess Eng. , vol.5 , pp. 219-226
    • Roy, S.K.1    Chiba, Y.2    Jigami, Y.3
  • 4
    • 33644835834 scopus 로고    scopus 로고
    • Glycosylation of natural and recombinant antibody molecules
    • Jefferis R. Glycosylation of natural and recombinant antibody molecules. Adv. Exp. Med. Biol. 564 (2005) 143-148
    • (2005) Adv. Exp. Med. Biol. , vol.564 , pp. 143-148
    • Jefferis, R.1
  • 5
    • 34249889580 scopus 로고    scopus 로고
    • Differences in the glycosylation profile of a monoclonal antibody produced by hybridomas cultured in serum-supplemented, serum-free, or chemically defined media
    • Serrato J.A., Hernandez V., Estrada-Mondaca S., Palomares L.A., and Ramirez O.T. Differences in the glycosylation profile of a monoclonal antibody produced by hybridomas cultured in serum-supplemented, serum-free, or chemically defined media. Biotechnol. Appl. Biochem. 47 (2007) 113-124
    • (2007) Biotechnol. Appl. Biochem. , vol.47 , pp. 113-124
    • Serrato, J.A.1    Hernandez, V.2    Estrada-Mondaca, S.3    Palomares, L.A.4    Ramirez, O.T.5
  • 6
    • 0034691229 scopus 로고    scopus 로고
    • Ammonium alters N-glycan structures of recombinant TNFR-IgG: degradative versus biosynthetic mechanisms
    • Gawlitzek M., Ryll T., Lofgren J., and Sliwkowski M.B. Ammonium alters N-glycan structures of recombinant TNFR-IgG: degradative versus biosynthetic mechanisms. Biotechnol. Bioeng. 68 (2000) 637-646
    • (2000) Biotechnol. Bioeng. , vol.68 , pp. 637-646
    • Gawlitzek, M.1    Ryll, T.2    Lofgren, J.3    Sliwkowski, M.B.4
  • 7
    • 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.I., and Papoutsakis E.T. Culture pH affects expression rates and glycosylation of recombinant mouse placental lactogen proteins by Chinese hamster ovary (CHO) cells. Biotechnology 11 (1993) 720-724
    • (1993) Biotechnology , vol.11 , pp. 720-724
    • Borys, M.C.1    Linzer, D.I.2    Papoutsakis, E.T.3
  • 9
    • 33947611087 scopus 로고    scopus 로고
    • Glycosylation of therapeutic proteins in different production systems
    • Werner R.G., Kopp K., and Schlueter M. Glycosylation of therapeutic proteins in different production systems. Acta Paediatr. Suppl. 96 (2007) 17-22
    • (2007) Acta Paediatr. Suppl. , vol.96 , pp. 17-22
    • Werner, R.G.1    Kopp, K.2    Schlueter, M.3
  • 10
    • 33847780791 scopus 로고    scopus 로고
    • Enhancement of erythropoietin production in recombinant Chinese hamster ovary cells by sodium lactate addition
    • Choi Y.S., Lee D.Y., Kim I.Y., Kim H.J., Park H.W., Choe T.B., and Kim I.H. Enhancement of erythropoietin production in recombinant Chinese hamster ovary cells by sodium lactate addition. Biotechnol. Bioprocess Eng. 12 (2007) 60-72
    • (2007) Biotechnol. Bioprocess Eng. , vol.12 , pp. 60-72
    • Choi, Y.S.1    Lee, D.Y.2    Kim, I.Y.3    Kim, H.J.4    Park, H.W.5    Choe, T.B.6    Kim, I.H.7
  • 11
    • 0028998769 scopus 로고
    • The asialoglycoprotein receptor: Relationships between structure, function, and expression
    • Stockert R.J. The asialoglycoprotein receptor: Relationships between structure, function, and expression. Physiol. Rev. 75 (1995) 591-609
    • (1995) Physiol. Rev. , vol.75 , pp. 591-609
    • Stockert, R.J.1
  • 12
    • 0038353923 scopus 로고    scopus 로고
    • Relationships between the N-glycan structures and biological activities of recombinant human erythropoietins produced using different culture conditions and purification procedures
    • Yuen C.T., Storring P.L., Tiplady R.J., Izquierdo M., Wait R., Gee C.K., Gerson P., Lloyd P., and Cremata J.A. Relationships between the N-glycan structures and biological activities of recombinant human erythropoietins produced using different culture conditions and purification procedures. Br. J. Haematol. 121 (2003) 511-526
    • (2003) Br. J. Haematol. , vol.121 , pp. 511-526
    • Yuen, C.T.1    Storring, P.L.2    Tiplady, R.J.3    Izquierdo, M.4    Wait, R.5    Gee, C.K.6    Gerson, P.7    Lloyd, P.8    Cremata, J.A.9
  • 14
    • 0036236811 scopus 로고    scopus 로고
    • N-Glycans stabilize human erythropoietin through hydrophobic interactions with the hydrophobic protein surface. Studies by surface plasmon resonance analysis
    • Toyoda T., Arakawa T., and Yamaguchi H. N-Glycans stabilize human erythropoietin through hydrophobic interactions with the hydrophobic protein surface. Studies by surface plasmon resonance analysis. J. Biochem. 131 (2002) 511-515
    • (2002) J. Biochem. , vol.131 , pp. 511-515
    • Toyoda, T.1    Arakawa, T.2    Yamaguchi, H.3
  • 15
    • 20444404610 scopus 로고    scopus 로고
    • Analysis of proteoglycans derived sulphated disaccharides by liquid chromatography/mass spectrometry
    • Barroso B., Didraga M., and Bischoff R. Analysis of proteoglycans derived sulphated disaccharides by liquid chromatography/mass spectrometry. J. Chromatogr. A 1080 (2005) 43-48
    • (2005) J. Chromatogr. A , vol.1080 , pp. 43-48
    • Barroso, B.1    Didraga, M.2    Bischoff, R.3
  • 16
    • 34547100984 scopus 로고    scopus 로고
    • High-performance liquid chromatographic/mass spectrometric studies on the susceptibility of heparin species to cleavage by heparanase
    • Bisio A., Mantegazza A., Urso E., Naggi A., Torri G., Viskov C., and Casu B. High-performance liquid chromatographic/mass spectrometric studies on the susceptibility of heparin species to cleavage by heparanase. Semin. Thromb. Hemost. 33 (2007) 488-495
    • (2007) Semin. Thromb. Hemost. , vol.33 , pp. 488-495
    • Bisio, A.1    Mantegazza, A.2    Urso, E.3    Naggi, A.4    Torri, G.5    Viskov, C.6    Casu, B.7
  • 18
    • 34748837881 scopus 로고    scopus 로고
    • Analysis of N-glycans from recombinant immunoglobulin G by on-line reversed-phase high-performance liquid chromatography/mass spectrometry
    • Chen X., and Flynn G.C. Analysis of N-glycans from recombinant immunoglobulin G by on-line reversed-phase high-performance liquid chromatography/mass spectrometry. Anal. Biochem. 370 (2007) 147-161
    • (2007) Anal. Biochem. , vol.370 , pp. 147-161
    • Chen, X.1    Flynn, G.C.2
  • 19
    • 33144464276 scopus 로고    scopus 로고
    • Glycoform quantification of chondroitin/dermatan sulfate using a liquid chromatography-tandem mass spectrometry platform
    • Hitchcock A.M., Costello C.E., and Zaia J. Glycoform quantification of chondroitin/dermatan sulfate using a liquid chromatography-tandem mass spectrometry platform. Biochemistry 45 (2006) 2350-2361
    • (2006) Biochemistry , vol.45 , pp. 2350-2361
    • Hitchcock, A.M.1    Costello, C.E.2    Zaia, J.3
  • 20
    • 25144521846 scopus 로고    scopus 로고
    • Quantification of isomers from a mixture of twelve heparin and heparan sulfate disaccharides using tandem mass spectrometry
    • Behr J.R., Matsumoto Y., White F.M., and Sasisekharan R. Quantification of isomers from a mixture of twelve heparin and heparan sulfate disaccharides using tandem mass spectrometry. Rapid Commun. Mass Spectrom. 19 (2005) 2553-2562
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 2553-2562
    • Behr, J.R.1    Matsumoto, Y.2    White, F.M.3    Sasisekharan, R.4
  • 22
    • 34547767471 scopus 로고    scopus 로고
    • Tags for the stable isotopic labeling of carbohydrates and quantitative analysis by mass spectrometry
    • Bowman M.J., and Zaia J. Tags for the stable isotopic labeling of carbohydrates and quantitative analysis by mass spectrometry. Anal. Chem. 79 (2007) 5777-5784
    • (2007) Anal. Chem. , vol.79 , pp. 5777-5784
    • Bowman, M.J.1    Zaia, J.2
  • 23
    • 45049083308 scopus 로고    scopus 로고
    • A relative and absolute quantification of neutral N-linked oligosaccharides using modification with carboxymethyl trimethylammonium hydrazide and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Gil G.C., Kim Y.G., and Kim B.G. A relative and absolute quantification of neutral N-linked oligosaccharides using modification with carboxymethyl trimethylammonium hydrazide and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal. Biochem. 379 (2008) 45-59
    • (2008) Anal. Biochem. , vol.379 , pp. 45-59
    • Gil, G.C.1    Kim, Y.G.2    Kim, B.G.3
  • 24
    • 0036012884 scopus 로고    scopus 로고
    • Derivatization of small oligosaccharides prior to analysis by matrix-assisted laser desorption/ionization using glycidyltrimethylammonium chloride and Girard's reagent T
    • Gouw J.W., Burgers P.C., Trikoupis M.A., and Terlouw J.K. Derivatization of small oligosaccharides prior to analysis by matrix-assisted laser desorption/ionization using glycidyltrimethylammonium chloride and Girard's reagent T. Rapid Commun. Mass Spectrom. 16 (2002) 905-912
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 905-912
    • Gouw, J.W.1    Burgers, P.C.2    Trikoupis, M.A.3    Terlouw, J.K.4
  • 25
    • 0000758635 scopus 로고    scopus 로고
    • Cationic derivatization of oligosaccharides with Girard's T reagent for improved performance in matrix-assisted laser desorption/ionization and electrospray mass spectrometry
    • Naven T.J.P., and Harvey D.J. Cationic derivatization of oligosaccharides with Girard's T reagent for improved performance in matrix-assisted laser desorption/ionization and electrospray mass spectrometry. Rapid Commun. Mass Spectrom. 10 (1996) 829-834
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , pp. 829-834
    • Naven, T.J.P.1    Harvey, D.J.2
  • 26
    • 0010040308 scopus 로고
    • Rapid and simultaneous methylation of fatty acids and hydroxy FA for gas chromatography analysis
    • Ciucanu I., and Kerek F. Rapid and simultaneous methylation of fatty acids and hydroxy FA for gas chromatography analysis. J. Chromatogr. 284 (1984) 179-185
    • (1984) J. Chromatogr. , vol.284 , pp. 179-185
    • Ciucanu, I.1    Kerek, F.2
  • 27
    • 0021424882 scopus 로고
    • Modification of sialic acid carboxyl group of ganglioside
    • Handa S., and Nakamura K. Modification of sialic acid carboxyl group of ganglioside. J. Biochem. 95 (1984) 1323-1329
    • (1984) J. Biochem. , vol.95 , pp. 1323-1329
    • Handa, S.1    Nakamura, K.2
  • 28
    • 0029164230 scopus 로고
    • Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid
    • Bigge J.C., Patel T.P., Bruce J.A., Goulding P.N., Charles S.M., and Parekh R.B. Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid. Anal. Biochem. 230 (1995) 229-238
    • (1995) Anal. Biochem. , vol.230 , pp. 229-238
    • Bigge, J.C.1    Patel, T.P.2    Bruce, J.A.3    Goulding, P.N.4    Charles, S.M.5    Parekh, R.B.6
  • 29
    • 46849116602 scopus 로고    scopus 로고
    • Quantitative derivatization of sialic acids for the detection of sialoglycans by MALDI MS
    • Toyoda M., Ito H., Matsuno Y.K., Narimatsu H., and Kameyama A. Quantitative derivatization of sialic acids for the detection of sialoglycans by MALDI MS. Anal. Chem. 80 (2008) 5211-5218
    • (2008) Anal. Chem. , vol.80 , pp. 5211-5218
    • Toyoda, M.1    Ito, H.2    Matsuno, Y.K.3    Narimatsu, H.4    Kameyama, A.5


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