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Volumn 19, Issue 11, 2008, Pages 1643-1654

Comparison of LC and LC/MS Methods for Quantifying N-Glycosylation in Recombinant IgGs

Author keywords

[No Author keywords available]

Indexed keywords

CHROMATOGRAPHIC ANALYSIS; ESTERIFICATION; GLYCOSYLATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; IONIZATION OF LIQUIDS; LIQUID CHROMATOGRAPHY; MASS SPECTROMETERS; MASS SPECTROMETRY;

EID: 55149085231     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jasms.2008.07.004     Document Type: Article
Times cited : (72)

References (25)
  • 1
    • 0032493848 scopus 로고    scopus 로고
    • Quantitative Analysis and Process Monitoring of Site-Specific Glycosylation Microheterogeneity in Recombinant Human Interferon-γ from Chinese Hamster Ovary Cell Culture by Hydrophilic Interaction Chromatography
    • Zhang J., and Wang D.I. Quantitative Analysis and Process Monitoring of Site-Specific Glycosylation Microheterogeneity in Recombinant Human Interferon-γ from Chinese Hamster Ovary Cell Culture by Hydrophilic Interaction Chromatography. J. Chromatogr. B Biomed. Sci. Appl. 712 (1998) 73-82
    • (1998) J. Chromatogr. B Biomed. Sci. Appl. , vol.712 , pp. 73-82
    • Zhang, J.1    Wang, D.I.2
  • 2
    • 0034045472 scopus 로고    scopus 로고
    • Comparisons of the Glycosylation of a Monoclonal Antibody Produced Under Nominally Identical Cell Culture Conditions in Two Different Bioreactors
    • Kunkel J.P., Jan D.C., Butler M., and Jamieson J.C. Comparisons of the Glycosylation of a Monoclonal Antibody Produced Under Nominally Identical Cell Culture Conditions in Two Different Bioreactors. Biotechnol. Prog. 16 (2000) 462-470
    • (2000) Biotechnol. Prog. , vol.16 , pp. 462-470
    • Kunkel, J.P.1    Jan, D.C.2    Butler, M.3    Jamieson, J.C.4
  • 4
    • 0032429137 scopus 로고    scopus 로고
    • The Effect on IgG Glycosylation of Altering β1, 4-galactosyltransferase-1 activity in B cells
    • Keusch J., Lydyard P.M., and Delves P.J. The Effect on IgG Glycosylation of Altering β1, 4-galactosyltransferase-1 activity in B cells. Glycobiology 8 (1998) 1215-1220
    • (1998) Glycobiology , vol.8 , pp. 1215-1220
    • Keusch, J.1    Lydyard, P.M.2    Delves, P.J.3
  • 6
    • 34748865088 scopus 로고    scopus 로고
    • Antibody Therapeutics: Isotype and Glycoform Selection
    • Jefferis R. Antibody Therapeutics: Isotype and Glycoform Selection. Expert Opin. Biol. Ther. 7 (2007) 1401-1413
    • (2007) Expert Opin. Biol. Ther. , vol.7 , pp. 1401-1413
    • Jefferis, R.1
  • 8
    • 0035081693 scopus 로고    scopus 로고
    • The Influence of Glycosylation on the Thermal Stability and Effector Function Expression of Human IgG1-Fc: Properties of a Series of Truncated Glycoforms
    • Mimura Y., Church S., Ghirlando R., Ashton P.R., Dong S., Goodall M., Lund J., and Jefferis R. The Influence of Glycosylation on the Thermal Stability and Effector Function Expression of Human IgG1-Fc: Properties of a Series of Truncated Glycoforms. Mol. Immunol. 37 (2000) 697-706
    • (2000) Mol. Immunol. , vol.37 , pp. 697-706
    • Mimura, Y.1    Church, S.2    Ghirlando, R.3    Ashton, P.R.4    Dong, S.5    Goodall, M.6    Lund, J.7    Jefferis, R.8
  • 9
    • 0037474543 scopus 로고    scopus 로고
    • Structural Analysis of Human IgG-Fc Glycoforms Reveals a Correlation Between Glycosylation and Structural Integrity
    • Krapp S., Mimura Y., Jefferis R., Huber R., and Sondermann P. Structural Analysis of Human IgG-Fc Glycoforms Reveals a Correlation Between Glycosylation and Structural Integrity. J. Mol. Biol. 325 (2003) 979-989
    • (2003) J. Mol. Biol. , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 12
    • 33746273552 scopus 로고    scopus 로고
    • Identification of Cysteinylation of a Free Cysteine in the Fab Region of a Recombinant Monoclonal IgG1 Antibody Using Lys-C Limited Proteolysis Coupled with LC/MS Analysis
    • Gadgil H.S., Bondarenko P.V., Pipes G.D., Dillon T.M., Banks D., Abel J., Kleemann G.R., and Treuheit M.J. Identification of Cysteinylation of a Free Cysteine in the Fab Region of a Recombinant Monoclonal IgG1 Antibody Using Lys-C Limited Proteolysis Coupled with LC/MS Analysis. Anal. Biochem. 355 (2006) 165-174
    • (2006) Anal. Biochem. , vol.355 , pp. 165-174
    • Gadgil, H.S.1    Bondarenko, P.V.2    Pipes, G.D.3    Dillon, T.M.4    Banks, D.5    Abel, J.6    Kleemann, G.R.7    Treuheit, M.J.8
  • 13
    • 33646398313 scopus 로고    scopus 로고
    • Improving Mass Accuracy of High Performance Liquid Chromatography/Electrospray Ionization Time-of-Flight Mass Spectrometry of Intact Antibodies
    • Gadgil H.S., Pipes G.D., Dillon T.M., Treuheit M.J., and Bondarenko P.V. Improving Mass Accuracy of High Performance Liquid Chromatography/Electrospray Ionization Time-of-Flight Mass Spectrometry of Intact Antibodies. J. Am. Soc. Mass Spectrom. 17 (2006) 867-872
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 867-872
    • Gadgil, H.S.1    Pipes, G.D.2    Dillon, T.M.3    Treuheit, M.J.4    Bondarenko, P.V.5
  • 15
    • 34548409568 scopus 로고    scopus 로고
    • Contrasting Glycosylation Profiles Between Fab and Fc of a Human IgG Protein Studied by Electrospray Ionization Mass Spectrometry
    • Mimura Y., Ashton P.R., Takahashi N., Harvey D.J., and Jefferis R. Contrasting Glycosylation Profiles Between Fab and Fc of a Human IgG Protein Studied by Electrospray Ionization Mass Spectrometry. J. Immunol. Methods 326 (2007) 116-126
    • (2007) J. Immunol. Methods , vol.326 , pp. 116-126
    • Mimura, Y.1    Ashton, P.R.2    Takahashi, N.3    Harvey, D.J.4    Jefferis, R.5
  • 16
    • 0035922885 scopus 로고    scopus 로고
    • Metabolic Control of Recombinant Monoclonal Antibody N-Glycosylation in GS-NS0 Cells
    • Hills A.E., Patel A., Boyd P., and James D.C. Metabolic Control of Recombinant Monoclonal Antibody N-Glycosylation in GS-NS0 Cells. Biotechnol. Bioeng. 75 (2001) 239-251
    • (2001) Biotechnol. Bioeng. , vol.75 , pp. 239-251
    • Hills, A.E.1    Patel, A.2    Boyd, P.3    James, D.C.4
  • 17
    • 37649019585 scopus 로고    scopus 로고
    • Reversed-Phase Liquid Chromatography-Mass Spectrometry of Site-Specific Chemical Modifications in Intact Immunoglobulin Molecules and Their Fragments
    • Ren D., Pipes G., Xiao G., Kleemann G.R., Bondarenko P.V., Treuheit M.J., and Gadgil H.S. Reversed-Phase Liquid Chromatography-Mass Spectrometry of Site-Specific Chemical Modifications in Intact Immunoglobulin Molecules and Their Fragments. J. Chromatogr. A 1179 (2007) 198-204
    • (2007) J. Chromatogr. A , vol.1179 , pp. 198-204
    • Ren, D.1    Pipes, G.2    Xiao, G.3    Kleemann, G.R.4    Bondarenko, P.V.5    Treuheit, M.J.6    Gadgil, H.S.7
  • 18
    • 36148998387 scopus 로고    scopus 로고
    • Reversed-Phase Liquid Chromatography of Immunoglobulin G Molecules and Their Fragments with the Diphenyl Column
    • Ren D., Pipes G.D., Hambly D.M., Bondarenko P.V., Treuheit M.J., Brems D.N., and Gadgil H.S. Reversed-Phase Liquid Chromatography of Immunoglobulin G Molecules and Their Fragments with the Diphenyl Column. J. Chromatogr. A 1175 (2007) 63-68
    • (2007) J. Chromatogr. A , vol.1175 , pp. 63-68
    • Ren, D.1    Pipes, G.D.2    Hambly, D.M.3    Bondarenko, P.V.4    Treuheit, M.J.5    Brems, D.N.6    Gadgil, H.S.7
  • 20
    • 0043011597 scopus 로고    scopus 로고
    • Kinetics of Whole Serum and Prepurified IgG Digestion by Pepsin for F(ab′)2 Manufacture
    • Boushaba R., Kumpalume P., and Slater N.K. Kinetics of Whole Serum and Prepurified IgG Digestion by Pepsin for F(ab′)2 Manufacture. Biotechnol. Prog. 19 (2003) 1176-1182
    • (2003) Biotechnol. Prog. , vol.19 , pp. 1176-1182
    • Boushaba, R.1    Kumpalume, P.2    Slater, N.K.3
  • 21
    • 0015021512 scopus 로고
    • The Products from Papain and Pepsin Hydrolyses of Guinea Pig Immunoglobulins γ-1G and γ-2 G
    • Leslie R.G., Melamed M.D., and Cohen S. The Products from Papain and Pepsin Hydrolyses of Guinea Pig Immunoglobulins γ-1G and γ-2 G. Biochem. J. 121 (1971) 829-837
    • (1971) Biochem. J. , vol.121 , pp. 829-837
    • Leslie, R.G.1    Melamed, M.D.2    Cohen, S.3
  • 23
    • 0035922885 scopus 로고    scopus 로고
    • Metabolic Control of Recombinant Monoclonal Antibody N-Glycosylation in GS-NS0 Cells
    • Hills A.E., Patel A., Boyd P., and James D.C. Metabolic Control of Recombinant Monoclonal Antibody N-Glycosylation in GS-NS0 Cells. Biotechnol. Bioeng. 75 (2001) 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
    • 33144484350 scopus 로고    scopus 로고
    • Determination and Characterization of Site-Specific N-Glycosylation Using MALDI-Qq-TOF Tandem Mass Spectrometry: Case Study with a Plant Protease
    • Bykova N.V., Rampitsch C., Krokhin O., Standing K.G., and Ens W. Determination and Characterization of Site-Specific N-Glycosylation Using MALDI-Qq-TOF Tandem Mass Spectrometry: Case Study with a Plant Protease. Anal. Chem. 78 (2006) 1093-1103
    • (2006) Anal. Chem. , vol.78 , pp. 1093-1103
    • Bykova, N.V.1    Rampitsch, C.2    Krokhin, O.3    Standing, K.G.4    Ens, W.5
  • 25
    • 0033655080 scopus 로고    scopus 로고
    • Characterization of Protein Glycosylation by MALDI-TOFMS
    • Mirgorodskaya E., Krogh T.N., and Roepstorff P. Characterization of Protein Glycosylation by MALDI-TOFMS. Methods Mol. Biol. 146 (2000) 273-292
    • (2000) Methods Mol. Biol. , vol.146 , pp. 273-292
    • Mirgorodskaya, E.1    Krogh, T.N.2    Roepstorff, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.