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Volumn 7, Issue 1, 2015, Pages 167-179

Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles - Part 1: Separation-based methods

Author keywords

2 ab labeling; Apts labeling; CE LIF; Dna analyzer; Glycan analysis; High throughput; HILIC UPLC; HPAEC; IgG glycosylation; Method comparison; Monoclonal antibody (mab)

Indexed keywords

2 AMINOBENZAMIDE; FLUORESCENT DYE; GLYCAN; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G; IMMUNOGLOBULIN G1 ANTIBODY; NAPHTHALENE DERIVATIVE; PYRENE DERIVATIVE; RECOMBINANT ANTIBODY; SIALIC ACID; SULFONIC ACID DERIVATIVE; MONOCLONAL ANTIBODY;

EID: 84921395878     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.4161/19420862.2014.986000     Document Type: Article
Times cited : (156)

References (70)
  • 1
    • 60849117560 scopus 로고    scopus 로고
    • Therapeutic antibodies and derivatives: From the bench to the clinic
    • PMID:19075681
    • Beck A, Wurch T, Corvaia N. Therapeutic antibodies and derivatives: from the bench to the clinic. Curr Pharm Biotechnol 2008; 9:421-2; PMID:19075681; http://dx.doi.org/10.2174/138920108786786420
    • (2008) Curr Pharm Biotechnol , vol.9 , pp. 421-422
    • Beck, A.1    Wurch, T.2    Corvaia, N.3
  • 2
    • 64949085560 scopus 로고    scopus 로고
    • Therapeutic antibodies: Current state and future trends-is a paradigm change coming soon?
    • PMID:19252861
    • Dimitrov DS, Marks JD. Therapeutic antibodies: current state and future trends-is a paradigm change coming soon? Methods Mol Biol 2009; 525:1-27, xiii; PMID:19252861; http://dx.doi.org/10.1007/978-1-59745-554-1-1
    • (2009) Methods Mol Biol , vol.525
    • Dimitrov, D.S.1    Marks, J.D.2
  • 4
    • 61649087668 scopus 로고    scopus 로고
    • Glycosylation as a strategy to improve antibody-based therapeutics
    • PMID:19247305
    • Jefferis R. Glycosylation as a strategy to improve antibody-based therapeutics. Nat Rev Drug Discov 2009; 8:226-34; PMID:19247305; http://dx.doi.org/10.1038/nrd2804
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 226-234
    • Jefferis, R.1
  • 5
    • 0029993902 scopus 로고    scopus 로고
    • Accessing the Kabat antibody sequence database by computer
    • PMID:8727325
    • Martin AC. Accessing the Kabat antibody sequence database by computer. Proteins 1996; 25:130-3; PMID:8727325; http://dx.doi.org/10.1002/(SICI)1097-0134(199605)25:1%3c130::AID-PROT11%3e3.3.CO;2-Y
    • (1996) Proteins , vol.25 , pp. 130-133
    • Martin, A.C.1
  • 6
    • 70449710875 scopus 로고    scopus 로고
    • Expression systems for therapeutic glycoprotein production
    • PMID:19889531
    • Durocher Y, Butler M. Expression systems for therapeutic glycoprotein production. Curr Opin Biotechnol 2009; 20:700-7; PMID:19889531; http://dx.doi.org/10.1016/j.copbio.2009.10.008
    • (2009) Curr Opin Biotechnol , vol.20 , pp. 700-707
    • Durocher, Y.1    Butler, M.2
  • 7
    • 60549114878 scopus 로고    scopus 로고
    • Glycosylation of antibody therapeutics: Optimisation for purpose
    • PMID:19183902
    • Jefferis R. Glycosylation of antibody therapeutics: optimisation for purpose. Methods Mol Biol 2009; 483:223-38; PMID:19183902; http://dx.doi.org/10.1007/978-1-59745-407-0-13
    • (2009) Methods Mol Biol , vol.483 , pp. 223-238
    • Jefferis, R.1
  • 9
    • 31844447560 scopus 로고    scopus 로고
    • Impact of variable domain glycosylation on antibody clearance: An LC/MS characterization
    • PMID:16360109
    • Huang L, Biolsi S, Bales KR, Kuchibhotla U. Impact of variable domain glycosylation on antibody clearance: an LC/MS characterization. Anal Biochem 2006; 349:197-207; PMID:16360109; http://dx.doi.org/10.1016/j.ab.2005.11.012
    • (2006) Anal Biochem , vol.349 , pp. 197-207
    • Huang, L.1    Biolsi, S.2    Bales, K.R.3    Kuchibhotla, U.4
  • 10
    • 40649109261 scopus 로고    scopus 로고
    • Glycosylation profiling of a therapeutic recombinant monoclonal antibody with two N-linked glycosylation sites using liquid chromatography coupled to a hybrid quadrupole time-of-flight mass spectrometer
    • PMID:18249181
    • Lim A, Reed-Bogan A, Harmon BJ. Glycosylation profiling of a therapeutic recombinant monoclonal antibody with two N-linked glycosylation sites using liquid chromatography coupled to a hybrid quadrupole time-of-flight mass spectrometer. Anal Biochem 2008; 375:163-72; PMID:18249181; http://dx.doi.org/10.1016/j.ab.2008.01.003
    • (2008) Anal Biochem , vol.375 , pp. 163-172
    • Lim, A.1    Reed-Bogan, A.2    Harmon, B.J.3
  • 11
    • 0029558207 scopus 로고
    • The effect of the removal of sialic acid, galactose and total carbohydrate on the functional activity of Campath-1H
    • PMID:8643100
    • Boyd PN, Lines AC, Patel AK. The effect of the removal of sialic acid, galactose and total carbohydrate on the functional activity of Campath-1H. Mol Immunol 1995; 32:1311-8; PMID:8643100; http://dx.doi.org/10.1016/0161-5890(95)00118-2
    • (1995) Mol Immunol , vol.32 , pp. 1311-1318
    • Boyd, P.N.1    Lines, A.C.2    Patel, A.K.3
  • 12
    • 84860911340 scopus 로고    scopus 로고
    • Quantitative evaluation of fucose reducing effects in a humanized antibody on Fcgamma receptor binding and antibody-dependent cell-mediated cytotoxicity activities
    • PMID:22531441
    • Chung S, Quarmby V, Gao X, Ying Y, Lin L, Reed C, Fong C, Lau W, Qiu ZJ, Shen A, et al. Quantitative evaluation of fucose reducing effects in a humanized antibody on Fcgamma receptor binding and antibody-dependent cell-mediated cytotoxicity activities. MAbs 2012; 4:326-40; PMID:22531441; http://dx.doi.org/10.4161/mabs.19941
    • (2012) MAbs , vol.4 , pp. 326-340
    • Chung, S.1    Quarmby, V.2    Gao, X.3    Ying, Y.4    Lin, L.5    Reed, C.6    Fong, C.7    Lau, W.8    Qiu, Z.J.9    Shen, A.10
  • 13
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • PMID:12427744
    • Shinkawa T, Nakamura K, Yamane N, Shoji-Hosaka E, Kanda Y, Sakurada M, Uchida K, Anazawa H, Satoh M, Yamasaki M, et al. The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J Biol Chem 2003; 278:3466-73; PMID:12427744; http://dx.doi.org/10.1074/jbc.M210665200
    • (2003) J Biol Chem , vol.278 , pp. 3466-3473
    • Shinkawa, T.1    Nakamura, K.2    Yamane, N.3    Shoji-Hosaka, E.4    Kanda, Y.5    Sakurada, M.6    Uchida, K.7    Anazawa, H.8    Satoh, M.9    Yamasaki, M.10
  • 15
    • 79958837668 scopus 로고    scopus 로고
    • High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans
    • PMID:21421994
    • Goetze AM, Liu YD, Zhang Z, Shah B, Lee E, Bondarenko PV, Flynn GC. High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans. Glycobiology 2011; 21:949-59; PMID:21421994; http://dx.doi.org/10.1093/glycob/cwr027
    • (2011) Glycobiology , vol.21 , pp. 949-959
    • Goetze, A.M.1    Liu, Y.D.2    Zhang, Z.3    Shah, B.4    Lee, E.5    Bondarenko, P.V.6    Flynn, G.C.7
  • 16
    • 79960046406 scopus 로고    scopus 로고
    • Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway
    • PMID:21685887
    • Anthony RM, Kobayashi T, Wermeling F, Ravetch JV. Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway. Nature 2011; 475: 110-3; PMID:21685887; http://dx.doi.org/10.1038/nature10134
    • (2011) Nature , vol.475 , pp. 110-113
    • Anthony, R.M.1    Kobayashi, T.2    Wermeling, F.3    Ravetch, J.V.4
  • 17
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • PMID:16888140
    • Kaneko Y, Nimmerjahn F, Ravetch JV. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 2006; 313:670-3; PMID:16888140; http://dx.doi.org/10.1126/science.1129594
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 19
    • 53049100695 scopus 로고    scopus 로고
    • Diversity in specificity, abundance, and composition of anti-Neu5Gc antibodies in normal humans: Potential implications for disease
    • PMID:18669916
    • Padler-Karavani V, Yu H, Cao H, Chokhawala H, Karp F, Varki N, Chen X, Varki A. Diversity in specificity, abundance, and composition of anti-Neu5Gc antibodies in normal humans: potential implications for disease. Glycobiology 2008; 18:818-30; PMID:18669916; http://dx.doi.org/10.1093/glycob/cwn072
    • (2008) Glycobiology , vol.18 , pp. 818-830
    • Padler-Karavani, V.1    Yu, H.2    Cao, H.3    Chokhawala, H.4    Karp, F.5    Varki, N.6    Chen, X.7    Varki, A.8
  • 20
    • 78650201043 scopus 로고    scopus 로고
    • Towards the implementation of quality by design to the production of therapeutic monoclonal antibodies with desired glycosylation patterns
    • PMID:20665659
    • del Val IJ, Kontoravdi C, Nagy JM. Towards the implementation of quality by design to the production of therapeutic monoclonal antibodies with desired glycosylation patterns. Biotechnol Prog 2010; 26:1505-27; PMID:20665659; http://dx.doi.org/10.1002/btpr.470
    • (2010) Biotechnol Prog , vol.26 , pp. 1505-1527
    • Del Val, I.J.1    Kontoravdi, C.2    Nagy, J.M.3
  • 22
    • 77956931053 scopus 로고    scopus 로고
    • A systematic approach to protein glycosylation analysis: A path through the maze
    • PMID:20852609
    • Marino K, Bones J, Kattla JJ, Rudd PM. A systematic approach to protein glycosylation analysis: a path through the maze. Nat Chem Biol 2010; 6:713-23; PMID:20852609; http://dx.doi.org/10.1038/nchembio.437
    • (2010) Nat Chem Biol , vol.6 , pp. 713-723
    • Marino, K.1    Bones, J.2    Kattla, J.J.3    Rudd, P.M.4
  • 23
    • 79551499066 scopus 로고    scopus 로고
    • Glycan analysis by modern instrumental methods
    • PMID:21241022
    • Pabst M, Altmann F. Glycan analysis by modern instrumental methods. Proteomics 2011; 11:631-43; PMID:21241022; http://dx.doi.org/10.1002/pmic.201000517
    • (2011) Proteomics , vol.11 , pp. 631-643
    • Pabst, M.1    Altmann, F.2
  • 24
    • 84883859087 scopus 로고    scopus 로고
    • Rapid Fc glycosylation analysis of Fc fusions with IdeS and liquid chromatography mass spectrometry
    • PMID:23839239
    • Lynaugh H, Li H, Gong B. Rapid Fc glycosylation analysis of Fc fusions with IdeS and liquid chromatography mass spectrometry. MAbs 2013; 5:641-5; PMID:23839239; http://dx.doi.org/10.4161/mabs.25302
    • (2013) MAbs , vol.5 , pp. 641-645
    • Lynaugh, H.1    Li, H.2    Gong, B.3
  • 25
    • 84876703111 scopus 로고    scopus 로고
    • Structural comparison of two anti-CD20 monoclonal antibody drug products using middledown mass spectrometry
    • PMID:23579346
    • Wang B, Gucinski AC, Keire DA, Buhse LF, Boyne MT, 2nd. Structural comparison of two anti-CD20 monoclonal antibody drug products using middledown mass spectrometry. Analyst 2013; 138:3058-65; PMID:23579346; http://dx.doi.org/10.1039/c3an36524g
    • (2013) Analyst , vol.138 , pp. 3058-3065
    • Wang, B.1    Gucinski, A.C.2    Keire, D.A.3    Buhse, L.F.4    Boyne, M.T.5
  • 26
    • 59149092065 scopus 로고    scopus 로고
    • Mass spectrometry for structural characterization of therapeutic antibodies
    • PMID:18720354
    • Zhang Z, Pan H, Chen X. Mass spectrometry for structural characterization of therapeutic antibodies. Mass Spectrom Rev 2009; 28:147-76; PMID:18720354; http://dx.doi.org/10.1002/mas.20190
    • (2009) Mass Spectrom Rev , vol.28 , pp. 147-176
    • Zhang, Z.1    Pan, H.2    Chen, X.3
  • 27
    • 78650351800 scopus 로고    scopus 로고
    • Ultra performance liquid chromatographic profiling of serum N-glycans for fast and efficient identification of cancer associated alterations in glycosylation
    • PMID:21073175
    • Bones J, Mittermayr S, O'Donoghue N, Guttman A, Rudd PM. Ultra performance liquid chromatographic profiling of serum N-glycans for fast and efficient identification of cancer associated alterations in glycosylation. Anal Chem 2010; 82:10208-15; PMID:21073175; http://dx.doi.org/10.1021/ac102860w
    • (2010) Anal Chem , vol.82 , pp. 10208-10215
    • Bones, J.1    Mittermayr, S.2    O'Donoghue, N.3    Guttman, A.4    Rudd, P.M.5
  • 28
    • 22244446150 scopus 로고    scopus 로고
    • Analysis of carbohydrates by anion exchange chromatography and mass spectrometry
    • PMID:16106855
    • Bruggink C, Maurer R, Herrmann H, Cavalli S, Hoefler F. Analysis of carbohydrates by anion exchange chromatography and mass spectrometry. J Chromatogr A 2005; 1085:104-9; PMID:16106855; http://dx.doi. org/10.1016/j.chroma.2005.03.108
    • (2005) J Chromatogr a , vol.1085 , pp. 104-109
    • Bruggink, C.1    Maurer, R.2    Herrmann, H.3    Cavalli, S.4    Hoefler, F.5
  • 29
    • 84868553080 scopus 로고    scopus 로고
    • High-throughput work flow for IgG Fc-glycosylation analysis of biotechnological samples
    • PMID:23026777
    • Reusch D, Haberger M, Selman MH, Bulau P, Deelder AM, Wuhrer M, Engler N. High-throughput work flow for IgG Fc-glycosylation analysis of biotechnological samples. Anal Biochem 2013; 432:82-9; PMID:23026777; http://dx.doi.org/10.1016/j.ab.2012.09.032
    • (2013) Anal Biochem , vol.432 , pp. 82-89
    • Reusch, D.1    Haberger, M.2    Selman, M.H.3    Bulau, P.4    Deelder, A.M.5    Wuhrer, M.6    Engler, N.7
  • 30
    • 76149085857 scopus 로고    scopus 로고
    • Immunoglobulin G glycopeptide profiling by matrix-assisted laser desorption ionization Fourier transform ion cyclotron resonance mass spectrometry
    • PMID:20058878
    • Selman MH, McDonnell LA, Palmblad M, Ruhaak LR, Deelder AM, Wuhrer M. Immunoglobulin G glycopeptide profiling by matrix-assisted laser desorption ionization Fourier transform ion cyclotron resonance mass spectrometry. Anal Chem 2010; 82:1073-81; PMID:20058878; http://dx.doi.org/10.1021/ac9024413
    • (2010) Anal Chem , vol.82 , pp. 1073-1081
    • Selman, M.H.1    McDonnell, L.A.2    Palmblad, M.3    Ruhaak, L.R.4    Deelder, A.M.5    Wuhrer, M.6
  • 31
    • 84901041505 scopus 로고    scopus 로고
    • LC-MS/MS peptide mapping with automated data processing for routine profiling of N-glycans in immunoglobulins
    • PMID:24664809
    • Shah B, Jiang XG, Chen L, Zhang Z. LC-MS/MS peptide mapping with automated data processing for routine profiling of N-glycans in immunoglobulins. J Am Soc Mass Spectrom 2014; 25:999-1011; PMID:24664809; http://dx.doi.org/10.1007/s13361-014-0858-3
    • (2014) J Am Soc Mass Spectrom , vol.25 , pp. 999-1011
    • Shah, B.1    Jiang, X.G.2    Chen, L.3    Zhang, Z.4
  • 32
    • 13244291497 scopus 로고    scopus 로고
    • Protein glycosylation analyzed by normal-phase nano-liquid chromatography-mass spectrometry of glycopeptides
    • PMID:15679358
    • Wuhrer M, Koeleman CA, Hokke CH, Deelder AM. Protein glycosylation analyzed by normal-phase nano-liquid chromatography-mass spectrometry of glycopeptides. Anal Chem 2005; 77:886-94; PMID:15679358; http://dx.doi.org/10.1021/ac048619x
    • (2005) Anal Chem , vol.77 , pp. 886-894
    • Wuhrer, M.1    Koeleman, C.A.2    Hokke, C.H.3    Deelder, A.M.4
  • 33
  • 34
    • 84901942411 scopus 로고    scopus 로고
    • Comparative performance of four methods for high-throughput glycosylation analysis of immunoglobulin G in genetic and epidemiological research
    • PMID:24719452
    • Huffman JE, Pucic-Bakovic M, Klaric L, Hennig R, Selman MH, Vuckovic F, Novokmet M, Krištić J, Borowiak M, Muth T, et al. Comparative performance of four methods for high-throughput glycosylation analysis of immunoglobulin G in genetic and epidemiological research. Mol Cell Proteomics 2014; 13:1598-610; PMID:24719452; http://dx.doi.org/10.1074/mcp.M113.037465
    • (2014) Mol Cell Proteomics , vol.13 , pp. 1598-1610
    • Huffman, J.E.1    Pucic-Bakovic, M.2    Klaric, L.3    Hennig, R.4    Selman, M.H.5    Vuckovic, F.6    Novokmet, M.7    Krištić, J.8    Borowiak, M.9    Muth, T.10
  • 35
    • 84885128443 scopus 로고    scopus 로고
    • Interlaboratory study on differential analysis of protein glycosylation by mass spectrometry: The ABRF glycoprotein research multi-institutional study 2012
    • PMID:23764502
    • Leymarie N, Griffin PJ, Jonscher K, Kolarich D, Orlando R, McComb M, Zaia J, Aguilan J, Alley WR, Altmann F, et al. Interlaboratory study on differential analysis of protein glycosylation by mass spectrometry: the ABRF glycoprotein research multi-institutional study 2012. Mol Cell Proteomics 2013; 12:2935-51; PMID:23764502; http://dx.doi.org/10.1074/mcp.M113.030643
    • (2013) Mol Cell Proteomics , vol.12 , pp. 2935-2951
    • Leymarie, N.1    Griffin, P.J.2    Jonscher, K.3    Kolarich, D.4    Orlando, R.5    McComb, M.6    Zaia, J.7    Aguilan, J.8    Alley, W.R.9    Altmann, F.10
  • 36
    • 55149085231 scopus 로고    scopus 로고
    • Comparison of LC and LC/MS methods for quantifying N-glycosylation in recombinant IgGs
    • PMID:18707900
    • Sinha S, Pipes G, Topp EM, Bondarenko PV, Treuheit MJ, Gadgil HS. Comparison of LC and LC/MS methods for quantifying N-glycosylation in recombinant IgGs. J Am Soc Mass Spectrom 2008; 19:1643-54; PMID:18707900; http://dx.doi.org/10.1016/j.jasms.2008.07.004
    • (2008) J Am Soc Mass Spectrom , vol.19 , pp. 1643-1654
    • Sinha, S.1    Pipes, G.2    Topp, E.M.3    Bondarenko, P.V.4    Treuheit, M.J.5    Gadgil, H.S.6
  • 37
    • 58949101498 scopus 로고    scopus 로고
    • Identification and quantification of N-linked oligosaccharides released from glycoproteins: An inter-laboratory study
    • PMID:18849584
    • Thobhani S, Yuen CT, Bailey MJ, Jones C. Identification and quantification of N-linked oligosaccharides released from glycoproteins: an inter-laboratory study. Glycobiology 2009; 19:201-11; PMID:18849584; http://dx.doi.org/10.1093/glycob/cwn099
    • (2009) Glycobiology , vol.19 , pp. 201-211
    • Thobhani, S.1    Yuen, C.T.2    Bailey, M.J.3    Jones, C.4
  • 38
    • 77950670724 scopus 로고    scopus 로고
    • Comparison of methods for profiling O-glycosylation: Human proteome organisation human disease glycomics/proteome initiative multi-institutional study of IgA1
    • PMID:20038609
    • Wada Y, Dell A, Haslam SM, Tissot B, Canis K, Azadi P, Bäckström M, Costello CE, Hansson GC, Hiki Y, et al. Comparison of methods for profiling O-glycosylation: human proteome organisation human disease glycomics/proteome initiative multi-institutional study of IgA1. Mol Cell Proteomics 2010; 9:719-27; PMID:20038609; http://dx.doi.org/10.1074/mcp.M900450-MCP200
    • (2010) Mol Cell Proteomics , vol.9 , pp. 719-727
    • Wada, Y.1    Dell, A.2    Haslam, S.M.3    Tissot, B.4    Canis, K.5    Azadi, P.6    Bäckström, M.7    Costello, C.E.8    Hansson, G.C.9    Hiki, Y.10
  • 40
    • 0028918220 scopus 로고
    • Separation of neutral asparagine-linked oligosaccharides by high-pH anion-exchange chromatography with pulsed amperometric detection
    • PMID:7785770
    • Cooper GA, Rohrer JS. Separation of neutral asparagine-linked oligosaccharides by high-pH anion-exchange chromatography with pulsed amperometric detection. Anal Biochem 1995; 226:182-4; PMID:7785770; http://dx.doi.org/10.1006/abio.1995.1207
    • (1995) Anal Biochem , vol.226 , pp. 182-184
    • Cooper, G.A.1    Rohrer, J.S.2
  • 41
    • 0030586330 scopus 로고    scopus 로고
    • The use of high-performance anion-exchange chromatography and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry to monitor and identify oligosaccharide degradation
    • PMID:8660630
    • Field M, Papac D, Jones A. The use of high-performance anion-exchange chromatography and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry to monitor and identify oligosaccharide degradation. Anal Biochem 1996; 239:92-8; PMID:8660630; http://dx.doi.org/10.1006/abio.1996.0295
    • (1996) Anal Biochem , vol.239 , pp. 92-98
    • Field, M.1    Papac, D.2    Jones, A.3
  • 42
    • 0342976375 scopus 로고
    • Separation of positional isomers of oligosaccharides and glycopeptides by high-performance anion-exchange chromatography with pulsed amperometric detection
    • PMID:3368440
    • Hardy MR, Townsend RR. Separation of positional isomers of oligosaccharides and glycopeptides by high-performance anion-exchange chromatography with pulsed amperometric detection. Proc Natl Acad Sci U S A 1988; 85:3289-93; PMID:3368440; http://dx.doi.org/10.1073/pnas.85.10.3289
    • (1988) Proc Natl Acad Sci U S a , vol.85 , pp. 3289-3293
    • Hardy, M.R.1    Townsend, R.R.2
  • 43
    • 43949107517 scopus 로고    scopus 로고
    • On-line CE-LIF-MS technology for the direct characterization of N-linked glycans from therapeutic antibodies
    • PMID:18426228
    • Gennaro LA, Salas-Solano O. On-line CE-LIF-MS technology for the direct characterization of N-linked glycans from therapeutic antibodies. Anal Chem 2008; 80:3838-45; PMID:18426228; http://dx.doi.org/10.1021/ac800152h
    • (2008) Anal Chem , vol.80 , pp. 3838-3845
    • Gennaro, L.A.1    Salas-Solano, O.2
  • 44
    • 0030064092 scopus 로고    scopus 로고
    • High-resolution capillary gel electrophoresis of reducing oligosaccharides labeled with 1-aminopyrene-3,6,8-trisulfonate
    • PMID:8789724
    • Guttman A, Chen FT, Evangelista RA, Cooke N. High-resolution capillary gel electrophoresis of reducing oligosaccharides labeled with 1-aminopyrene-3,6,8-trisulfonate. Anal Biochem 1996; 233:234-42; PMID:8789724; http://dx.doi.org/10.1006/abio.1996.0034
    • (1996) Anal Biochem , vol.233 , pp. 234-242
    • Guttman, A.1    Chen, F.T.2    Evangelista, R.A.3    Cooke, N.4
  • 45
    • 0028884861 scopus 로고
    • Capillary gel electrophoresis separation of high-mannose type oligosaccharides derivatized by 1-aminopyrene-3,6,8-trisulfonic acid
    • PMID:8586063
    • Guttman A, Pritchett T. Capillary gel electrophoresis separation of high-mannose type oligosaccharides derivatized by 1-aminopyrene-3,6,8-trisulfonic acid. Electrophoresis 1995; 16:1906-11; PMID:8586063; http://dx.doi.org/10.1002/elps.11501601314
    • (1995) Electrophoresis , vol.16 , pp. 1906-1911
    • Guttman, A.1    Pritchett, T.2
  • 46
    • 84858976069 scopus 로고    scopus 로고
    • Alignment of laser-induced fluorescence and mass spectrometric detection traces using electrophoretic mobility scaling in CELIF-MS of labeled N-glycans
    • PMID:22451048
    • Huhn C, Ruhaak LR, Mannhardt J, Wuhrer M, Neususs C, Deelder AM, Meyer H. Alignment of laser-induced fluorescence and mass spectrometric detection traces using electrophoretic mobility scaling in CELIF-MS of labeled N-glycans. Electrophoresis 2012; 33:563-6; PMID:22451048; http://dx.doi.org/10.1002/elps.201100367
    • (2012) Electrophoresis , vol.33 , pp. 563-566
    • Huhn, C.1    Ruhaak, L.R.2    Mannhardt, J.3    Wuhrer, M.4    Neususs, C.5    Deelder, A.M.6    Meyer, H.7
  • 47
    • 84877350385 scopus 로고    scopus 로고
    • Unraveling the glyco-puzzle: Glycan structure identification by capillary electrophoresis
    • PMID:23560607
    • Mittermayr S, Bones J, Guttman A. Unraveling the glyco-puzzle: glycan structure identification by capillary electrophoresis. Anal Chem 2013; 85:4228-38; PMID:23560607; http://dx.doi.org/10.1021/ac4006099
    • (2013) Anal Chem , vol.85 , pp. 4228-4238
    • Mittermayr, S.1    Bones, J.2    Guttman, A.3
  • 48
    • 78649869061 scopus 로고    scopus 로고
    • Optimized workflow for preparation of APTS-labeled N-glycans allowing high-throughput analysis of human plasma glycomes using 48-channel multiplexed CGE-LIF
    • PMID:20886907
    • Ruhaak LR, Hennig R, Huhn C, Borowiak M, Dolhain RJ, Deelder AM, Rapp E, Wuhrer M. Optimized workflow for preparation of APTS-labeled N-glycans allowing high-throughput analysis of human plasma glycomes using 48-channel multiplexed CGE-LIF. J Proteome Res 2010; 9:6655-64; PMID:20886907; http://dx.doi.org/10.1021/pr100802f
    • (2010) J Proteome Res , vol.9 , pp. 6655-6664
    • Ruhaak, L.R.1    Hennig, R.2    Huhn, C.3    Borowiak, M.4    Dolhain, R.J.5    Deelder, A.M.6    Rapp, E.7    Wuhrer, M.8
  • 49
    • 84887664948 scopus 로고    scopus 로고
    • Capillary electrophoresis/mass spectrometry of APTS-labeled glycans for the identification of unknown glycan species in capillary electrophoresis/laser-induced fluorescence systems
    • PMID:24024676
    • Bunz SC, Rapp E, Neususs C. Capillary electrophoresis/mass spectrometry of APTS-labeled glycans for the identification of unknown glycan species in capillary electrophoresis/laser-induced fluorescence systems. Anal Chem 2013; 85:10218-24; PMID:24024676; http://dx.doi.org/10.1021/ac401930j
    • (2013) Anal Chem , vol.85 , pp. 10218-10224
    • Bunz, S.C.1    Rapp, E.2    Neususs, C.3
  • 50
    • 8344290478 scopus 로고    scopus 로고
    • Total serum protein N-glycome profiling on a capillary electrophoresis-microfluidics platform
    • PMID:15472972
    • Callewaert N, Contreras R, Mitnik-Gankin L, Carey L, Matsudaira P, Ehrlich D. Total serum protein N-glycome profiling on a capillary electrophoresis-microfluidics platform. Electrophoresis 2004; 25:3128-31; PMID:15472972; http://dx.doi.org/10.1002/elps.200406020
    • (2004) Electrophoresis , vol.25 , pp. 3128-3131
    • Callewaert, N.1    Contreras, R.2    Mitnik-Gankin, L.3    Carey, L.4    Matsudaira, P.5    Ehrlich, D.6
  • 51
    • 0034948464 scopus 로고    scopus 로고
    • Ultrasensitive profiling and sequencing of N-linked oligosaccharides using standard DNA-sequencing equipment
    • PMID:11358876
    • Callewaert N, Geysens S, Molemans F, Contreras R. Ultrasensitive profiling and sequencing of N-linked oligosaccharides using standard DNA-sequencing equipment. Glycobiology 2001; 11:275-81; PMID:11358876; http://dx.doi.org/10.1093/glycob/11.4.275
    • (2001) Glycobiology , vol.11 , pp. 275-281
    • Callewaert, N.1    Geysens, S.2    Molemans, F.3    Contreras, R.4
  • 52
    • 1942454310 scopus 로고    scopus 로고
    • Noninvasive diagnosis of liver cirrhosis using DNA sequencer-based total serum protein glycomics
    • PMID:15152612
    • Callewaert N, Van Vlierberghe H, Van Hecke A, Laroy W, Delanghe J, Contreras R. Noninvasive diagnosis of liver cirrhosis using DNA sequencer-based total serum protein glycomics. Nat Med 2004; 10:429-34; PMID:15152612; http://dx.doi.org/10.1038/nm1006
    • (2004) Nat Med , vol.10 , pp. 429-434
    • Callewaert, N.1    Van Vlierberghe, H.2    Van Hecke, A.3    Laroy, W.4    Delanghe, J.5    Contreras, R.6
  • 53
    • 84892577275 scopus 로고    scopus 로고
    • High-throughput glycosylation analysis of therapeutic immunoglobulin G by capillary gel electrophoresis using a DNA analyzer
    • PMID:24135630
    • Reusch D, Haberger M, Kailich T, Heidenreich AK, Kampe M, Bulau P, Wuhrer M. High-throughput glycosylation analysis of therapeutic immunoglobulin G by capillary gel electrophoresis using a DNA analyzer. MAbs 2014; 6:185-96; PMID:24135630; http://dx.doi.org/10.4161/mabs.26712
    • (2014) MAbs , vol.6 , pp. 185-196
    • Reusch, D.1    Haberger, M.2    Kailich, T.3    Heidenreich, A.K.4    Kampe, M.5    Bulau, P.6    Wuhrer, M.7
  • 54
    • 56849090276 scopus 로고    scopus 로고
    • N-glycan analysis by CGE-LIF: Profiling influenza a virus hemagglutinin N-glycosylation during vaccine production
    • PMID:18925582
    • Schwarzer J, Rapp E, Reichl U. N-glycan analysis by CGE-LIF: profiling influenza a virus hemagglutinin N-glycosylation during vaccine production. Electrophoresis 2008; 29:4203-14; PMID:18925582; http://dx.doi.org/10.1002/elps.200800042
    • (2008) Electrophoresis , vol.29 , pp. 4203-4214
    • Schwarzer, J.1    Rapp, E.2    Reichl, U.3
  • 55
    • 74049141466 scopus 로고    scopus 로고
    • Separation of 2-aminobenzamide labeled glycans using hydrophilic interaction chromatography columns packed with 1.7 microm sorbent
    • PMID:20036624
    • Ahn J, Bones J, Yu YQ, Rudd PM, Gilar M. Separation of 2-aminobenzamide labeled glycans using hydrophilic interaction chromatography columns packed with 1.7 microm sorbent. J Chromatogr B Analyt Technol Biomed Life Sci 2010; 878:403-8; PMID:20036624; http://dx.doi.org/10.1016/j.jchromb.2009.12.013
    • (2010) J Chromatogr B Analyt Technol Biomed Life Sci , vol.878 , pp. 403-408
    • Ahn, J.1    Bones, J.2    Yu, Y.Q.3    Rudd, P.M.4    Gilar, M.5
  • 56
    • 0031820069 scopus 로고    scopus 로고
    • High resolution and high sensitivity methods for oligosaccharide mapping and characterization by normal phase high performance liquid chromatography following derivatization with highly fluorescent anthranilic acid
    • PMID:9621109
    • Anumula KR, Dhume ST. High resolution and high sensitivity methods for oligosaccharide mapping and characterization by normal phase high performance liquid chromatography following derivatization with highly fluorescent anthranilic acid. Glycobiology 1998; 8:685-94; PMID:9621109; http://dx.doi.org/10.1093/glycob/8.7.685
    • (1998) Glycobiology , vol.8 , pp. 685-694
    • Anumula, K.R.1    Dhume, S.T.2
  • 57
    • 0029164230 scopus 로고
    • Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid
    • PMID:7503412
    • Bigge JC, Patel TP, Bruce JA, Goulding PN, Charles SM, Parekh RB. Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid. Anal Biochem 1995; 230:229-38; PMID:7503412; http://dx.doi.org/10.1006/abio.1995.1468
    • (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
  • 59
    • 34447310112 scopus 로고    scopus 로고
    • Detailed structural analysis of N-glycans released from glycoproteins in SDS-PAGE gel bands using HPLC combined with exoglycosidase array digestions
    • PMID:17072008
    • Royle L, Radcliffe CM, Dwek RA, Rudd PM. Detailed structural analysis of N-glycans released from glycoproteins in SDS-PAGE gel bands using HPLC combined with exoglycosidase array digestions. Methods Mol Biol 2006; 347:125-43; PMID:17072008
    • (2006) Methods Mol Biol , vol.347 , pp. 125-143
    • Royle, L.1    Radcliffe, C.M.2    Dwek, R.A.3    Rudd, P.M.4
  • 60
    • 84861231265 scopus 로고    scopus 로고
    • Analysis of urinary oligosaccharides in lysosomal storage disorders by capillary high-performance anion-exchange chromatography-mass spectrometry
    • PMID:22526647
    • Bruggink C, Poorthuis BJ, Deelder AM, Wuhrer M. Analysis of urinary oligosaccharides in lysosomal storage disorders by capillary high-performance anion-exchange chromatography-mass spectrometry. Anal Bioanal Chem 2012; 403:1671-83; PMID:22526647; http://dx.doi.org/10.1007/s00216-012-5968-9
    • (2012) Anal Bioanal Chem , vol.403 , pp. 1671-1683
    • Bruggink, C.1    Poorthuis, B.J.2    Deelder, A.M.3    Wuhrer, M.4
  • 61
    • 79951838374 scopus 로고    scopus 로고
    • NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic
    • PMID:21258329
    • Barb AW, Prestegard JH. NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic. Nat Chem Biol 2011; 7:147-53; PMID:21258329; http://dx.doi.org/10.1038/nchembio.511
    • (2011) Nat Chem Biol , vol.7 , pp. 147-153
    • Barb, A.W.1    Prestegard, J.H.2
  • 62
    • 0029445206 scopus 로고
    • Comparison of fragmentation modes for the structural determination of complex oligosaccharides ionized by matrix-assisted laser desorption/ionization mass spectrometry
    • PMID:8652879
    • Harvey DJ, Naven TJ, Kuster B, Bateman RH, Green MR, Critchley G. Comparison of fragmentation modes for the structural determination of complex oligosaccharides ionized by matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun Mass Spectrom 1995; 9:1556-61; PMID:8652879; http://dx.doi.org/10.1002/rcm.1290091517
    • (1995) Rapid Commun Mass Spectrom , vol.9 , pp. 1556-1561
    • Harvey, D.J.1    Naven, T.J.2    Kuster, B.3    Bateman, R.H.4    Green, M.R.5    Critchley, G.6
  • 63
    • 0025290953 scopus 로고
    • A comparative study of the N-linked oligosaccharide structures of human IgG subclass proteins
    • PMID:2363690
    • Jefferis R, Lund J, Mizutani H, Nakagawa H, Kawazoe Y, Arata Y, Takahashi N. A comparative study of the N-linked oligosaccharide structures of human IgG subclass proteins. Biochem J 1990; 268:529-37; PMID:2363690
    • (1990) Biochem J , vol.268 , pp. 529-537
    • Jefferis, R.1    Lund, J.2    Mizutani, H.3    Nakagawa, H.4    Kawazoe, Y.5    Arata, Y.6    Takahashi, N.7
  • 64
    • 0021354983 scopus 로고
    • Branch specificity of purified rat liver Golgi UDP-galactose: N-acetylglucosamine beta-1,4-galactosyl-transferase. Preferential transfer of of galactose on the GlcNAc beta 1,2-Man alpha 1,3-branch of a complex biantennary Asn-linked oligosaccharide
    • PMID:6425277
    • Paquet MR, Narasimhan S, Schachter H, Moscarello MA. Branch specificity of purified rat liver Golgi UDP-galactose: N-acetylglucosamine beta-1,4-galactosyl-transferase. Preferential transfer of of galactose on the GlcNAc beta 1,2-Man alpha 1,3-branch of a complex biantennary Asn-linked oligosaccharide. J Biol Chem 1984; 259:4716-21; PMID:6425277
    • (1984) J Biol Chem , vol.259 , pp. 4716-4721
    • Paquet, M.R.1    Narasimhan, S.2    Schachter, H.3    Moscarello, M.A.4
  • 65
    • 0034050074 scopus 로고    scopus 로고
    • Species-specific variation in glycosylation of IgG: Evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics
    • PMID:10764836
    • Raju TS, Briggs JB, Borge SM, Jones AJ. Species-specific variation in glycosylation of IgG: evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics. Glycobiology 2000; 10:477-86; PMID:10764836; http://dx.doi.org/10.1093/glycob/10.5.477
    • (2000) Glycobiology , vol.10 , pp. 477-486
    • Raju, T.S.1    Briggs, J.B.2    Borge, S.M.3    Jones, A.J.4
  • 66
    • 0031028909 scopus 로고    scopus 로고
    • Variations in oligosaccharide-protein interactions in immunoglobulin G determine the site-specific glycosylation profiles and modulate the dynamic motion of the Fc oligosaccharides
    • PMID:9063885
    • Wormald MR, Rudd PM, Harvey DJ, Chang SC, Scragg IG, Dwek RA. Variations in oligosaccharide-protein interactions in immunoglobulin G determine the site-specific glycosylation profiles and modulate the dynamic motion of the Fc oligosaccharides. Biochemistry 1997; 36:1370-80; PMID:9063885; http://dx.doi.org/10.1021/bi9621472
    • (1997) Biochemistry , vol.36 , pp. 1370-1380
    • Wormald, M.R.1    Rudd, P.M.2    Harvey, D.J.3    Chang, S.C.4    Scragg, I.G.5    Dwek, R.A.6
  • 67
    • 0030839756 scopus 로고    scopus 로고
    • Rapid, sensitive sequencing of oligosaccharides from glycoproteins
    • PMID:9265730
    • Rudd PM, Dwek RA. Rapid, sensitive sequencing of oligosaccharides from glycoproteins. Curr Opin Biotechnol 1997; 8:488-97; PMID:9265730; http://dx.doi.org/10.1016/S0958-1669(97)80073-0
    • (1997) Curr Opin Biotechnol , vol.8 , pp. 488-497
    • Rudd, P.M.1    Dwek, R.A.2
  • 68
    • 67249087592 scopus 로고    scopus 로고
    • Development of a high performance anion exchange chromatography analysis for mapping of oligosaccharides
    • PMID:19482525
    • Grey C, Edebrink P, Krook M, Jacobsson SP. Development of a high performance anion exchange chromatography analysis for mapping of oligosaccharides. J Chromatogr B Analyt Technol Biomed Life Sci 2009; 877:1827-32; PMID:19482525; http://dx.doi.org/10.1016/j.jchromb.2009.05.003
    • (2009) J Chromatogr B Analyt Technol Biomed Life Sci , vol.877 , pp. 1827-1832
    • Grey, C.1    Edebrink, P.2    Krook, M.3    Jacobsson, S.P.4
  • 69
    • 0023752198 scopus 로고
    • High-performance anion-exchange chromatography of oligosaccharides using pellicular resins and pulsed amperometric detection
    • PMID:3239749
    • Townsend RR, Hardy MR, Hindsgaul O, Lee YC. High-performance anion-exchange chromatography of oligosaccharides using pellicular resins and pulsed amperometric detection. Anal Biochem 1988; 174:459-70; PMID:3239749; http://dx.doi.org/10.1016/0003-2697(88)90044-9
    • (1988) Anal Biochem , vol.174 , pp. 459-470
    • Townsend, R.R.1    Hardy, M.R.2    Hindsgaul, O.3    Lee, Y.C.4
  • 70
    • 0033044588 scopus 로고    scopus 로고
    • Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity
    • PMID:10052355
    • Umana P, Jean-Mairet J, Moudry R, Amstutz H, Bailey JE. Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity. Nat Biotechnol 1999; 17:176-80; PMID:10052355; http://dx.doi.org/10.1038/6179
    • (1999) Nat Biotechnol , vol.17 , pp. 176-180
    • Umana, P.1    Jean-Mairet, J.2    Moudry, R.3    Amstutz, H.4    Bailey, J.E.5


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