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Volumn , Issue , 2009, Pages 525-540

Molecular and Functional Characterization of Monoclonal Antibodies

Author keywords

Glycosylation and glycan analysis enzymatic release of N linked glycans; Molecular and functional characterization of monoclonal antibodies; Molecular heterogeneity

Indexed keywords


EID: 84890970713     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470485408.ch23     Document Type: Chapter
Times cited : (9)

References (41)
  • 2
    • 0035943486 scopus 로고    scopus 로고
    • Affinity-reversed phase liquid chromatography assay to quantitate recombinant antibodies and antibody fragments in fermentation broth
    • Battersby, J.E., B. Snedecor, C. Chen, K.M. Champion, L. Riddle, and M. Vanderlaan. 2001. Affinity-reversed phase liquid chromatography assay to quantitate recombinant antibodies and antibody fragments in fermentation broth. J. Chromatogr. A 927:61-76.
    • (2001) J. Chromatogr. A , vol.927 , pp. 61-76
    • Battersby, J.E.1    Snedecor, B.2    Chen, C.3    Champion, K.M.4    Riddle, L.5    Vanderlaan, M.6
  • 3
    • 0029164230 scopus 로고
    • Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid
    • Bigge, J.C., T.P. Patel, J.A. Bruce, P.N. Goulding, S.M. Charles, and R.B. Parekh. 1995. Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid. Anal. Biochem. 230(2):229-238.
    • (1995) Anal. Biochem , vol.230 , Issue.2 , 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
  • 4
    • 0030022071 scopus 로고    scopus 로고
    • Isomerization of an aspartic acid residue in the complementarity-determining regions of a recombinant antibody to human IgE: Identification and effect on binding affinity
    • Cacia, J., R. Keck, L.G. Presta, and J. Frenz. 1996. Isomerization of an aspartic acid residue in the complementarity-determining regions of a recombinant antibody to human IgE: Identification and effect on binding affinity. Biochemistry 35:1897-1903.
    • (1996) Biochemistry , vol.35 , pp. 1897-1903
    • Cacia, J.1    Keck, R.2    Presta, L.G.3    Frenz, J.4
  • 5
    • 33645697563 scopus 로고    scopus 로고
    • Formation of pyroglutamic acid from N-terminal glutamic acid in immunoglobulin gamma antibodies
    • Chelius, D., et al. 2006. Formation of pyroglutamic acid from N-terminal glutamic acid in immunoglobulin gamma antibodies. Anal. Chem. 78(7):2370-2376.
    • (2006) Anal. Chem , vol.78 , Issue.7 , pp. 2370-2376
    • Chelius, D.1
  • 6
    • 8344224534 scopus 로고    scopus 로고
    • Characterizing biological products and assessing comparability following manufacturing changes
    • Chirino, A.J., and Mire-Sluis, A. 2004. Characterizing biological products and assessing comparability following manufacturing changes. Nature Biotechnol. 22:1383-1391.
    • (2004) Nature Biotechnol , vol.22 , pp. 1383-1391
    • Chirino, A.J.1    Mire-Sluis, A.2
  • 7
    • 34247346055 scopus 로고    scopus 로고
    • Comparison of methionine oxidation in thermal stability and chemically stressed samples of a fully human monoclonal antibody
    • Chumsae, C., et al. 2007. Comparison of methionine oxidation in thermal stability and chemically stressed samples of a fully human monoclonal antibody. J. Chromatogr. B 850(1-2):285-294.
    • (2007) J. Chromatogr. B , vol.850 , Issue.1-2 , pp. 285-294
    • Chumsae, C.1
  • 8
    • 34250182367 scopus 로고    scopus 로고
    • Beta-elimination and peptide bond hydrolysis: Two distinct mechanisms of human IgG1 hinge fragmentation upon storage
    • Cohen, S.L., C. Price, and J. Vlasak. 2007. Beta-elimination and peptide bond hydrolysis: Two distinct mechanisms of human IgG1 hinge fragmentation upon storage. J. Am. Chem. Soc. 129:6976-6977.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 6976-6977
    • Cohen, S.L.1    Price, C.2    Vlasak, J.3
  • 10
    • 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, M.H., D.C. James, M. Rendall, A.P. Ison, M. Hoare, and A.T. Bull. 1998. Monitoring recombinant human interferon-gamma N-glycosylation during perfused fluidized-bed and stirred-tank batch culture of CHO cells. Biotechnol. Bioeng. 60(5):596-607.
    • (1998) Biotechnol. Bioeng , vol.60 , Issue.5 , 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
  • 11
    • 0036882287 scopus 로고    scopus 로고
    • Protein disulfide bond determination by mass spectrometry
    • Gorman, J.J., T.P. Wallis, and J.J. Pitt. 2002. Protein disulfide bond determination by mass spectrometry. Mass Spectrometry Rev. 21(3):183-216.
    • (2002) Mass Spectrometry Rev , vol.21 , Issue.3 , pp. 183-216
    • Gorman, J.J.1    Wallis, T.P.2    Pitt, J.J.3
  • 12
    • 0027445423 scopus 로고
    • Assessing genetic heterogeneity in production cell lines: Detection by peptide mapping of a low level Tyr to Gln sequence variant in a recombinant antibody
    • Harris, R.J., A.A. Murnane, S.L. Utter, K.L. Wagner, E.T. Cox, G. Polastri, J.C. Helder, and M.B. Sliwkowski. 1993. Assessing genetic heterogeneity in production cell lines: Detection by peptide mapping of a low level Tyr to Gln sequence variant in a recombinant antibody. Biotechnology 11:1293-1297.
    • (1993) Biotechnology , vol.11 , pp. 1293-1297
    • Harris, R.J.1    Murnane, A.A.2    Utter, S.L.3    Wagner, K.L.4    Cox, E.T.5    Polastri, G.6    Helder, J.C.7    Sliwkowski, M.B.8
  • 13
    • 3843058933 scopus 로고    scopus 로고
    • Commercial manufacturing scale formulation and analytical characterization of therapeutic recombinant antibodies
    • Harris, R.J., S.J. Shire, and C. Winter. 2004. Commercial manufacturing scale formulation and analytical characterization of therapeutic recombinant antibodies. Drug Dev. Res. 61:17.
    • (2004) Drug Dev. Res , vol.61 , pp. 17
    • Harris, R.J.1    Shire, S.J.2    Winter, C.3
  • 14
    • 0030338341 scopus 로고    scopus 로고
    • Characterization, formulation, and stability of Neupogen (filgras-tim), a recombinant human granulocyte colony-stimulating factor
    • In, ed. R. Pearlman and Y.J. Wang,, New York: Plenum Press.
    • Herman, A.C., T.C. Boone, and H.S. Lu. 1996. Characterization, formulation, and stability of Neupogen (filgras-tim), a recombinant human granulocyte colony-stimulating factor. In Formulation, Characterization, and Stability of Protein Drugs, ed. R. Pearlman and Y.J. Wang, 303-328. New York: Plenum Press.
    • (1996) Formulation, Characterization, and Stability of Protein Drugs , pp. 303-328
    • Herman, A.C.1    Boone, T.C.2    Lu, H.S.3
  • 15
    • 27744566590 scopus 로고    scopus 로고
    • Determination of picomolar equilibrium dissociation constants in solution by enzyme-linked immunosorbent assay with fluorescence detection
    • High, K., Y. Meng, M. Washabaugh, and Q. Zhao. 2005. Determination of picomolar equilibrium dissociation constants in solution by enzyme-linked immunosorbent assay with fluorescence detection. Anal. Biochem 347:159-161.
    • (2005) Anal. Biochem , vol.347 , pp. 159-161
    • High, K.1    Meng, Y.2    Washabaugh, M.3    Zhao, Q.4
  • 16
    • 0034802701 scopus 로고    scopus 로고
    • Glycosylation of human IgG antibodies: Relevance to theraputic applications
    • Jefferis, R. 2001. Glycosylation of human IgG antibodies: Relevance to theraputic applications. BioPharm (International) 14:19-26.
    • (2001) BioPharm (International) , vol.14 , pp. 19-26
    • Jefferis, R.1
  • 17
    • 0034584873 scopus 로고    scopus 로고
    • The use of circular dichroism in the investigation of protein structure and function
    • Kelly, S.M., and N.C. Price. 2000. The use of circular dichroism in the investigation of protein structure and function. Curr. Protein Pept. Sci. 1:349-384.
    • (2000) Curr. Protein Pept. Sci , vol.1 , pp. 349-384
    • Kelly, S.M.1    Price, N.C.2
  • 18
    • 32344449790 scopus 로고    scopus 로고
    • Optimization of humanized IgGs in glycoengineered Pichia pastoris
    • Li, H., N. Sethuraman, T.A. Stadheim, et al. 2006. Optimization of humanized IgGs in glycoengineered Pichia pastoris. Nature Biotechnol. 24(2):210-215.
    • (2006) Nature Biotechnol , vol.24 , Issue.2 , pp. 210-215
    • Li, H.1    Sethuraman, N.2    Stadheim, T.A.3
  • 19
    • 40649109261 scopus 로고    scopus 로고
    • Glycosylation profiling of atherapeutic recombinant monoclonal antibody with two N-linked glycosylation sites using liquid chromatography coupled to a hybrid quadrupole time-of-flight mass spectrometer
    • Lim, A., A. Reed-Bogan, and B.J. Harmon. 2008. Glycosylation profiling of atherapeutic recombinant monoclonal antibody with two N-linked glycosylation sites using liquid chromatography coupled to a hybrid quadrupole time-of-flight mass spectrometer. Anal. Biochem. 375(2):163-172.
    • (2008) Anal. Biochem , vol.375 , Issue.2 , pp. 163-172
    • Lim, A.1    Reed-Bogan, A.2    Harmon, B.J.3
  • 20
    • 33747099227 scopus 로고    scopus 로고
    • Effect of posttranslational modifications on the thermal stability of a recombinant monoclonal antibody
    • Liu, H., et al. 2006. Effect of posttranslational modifications on the thermal stability of a recombinant monoclonal antibody. Immunol. Lett. 106(2):144-153.
    • (2006) Immunol. Lett , vol.106 , Issue.2 , pp. 144-153
    • Liu, H.1
  • 21
    • 52449112071 scopus 로고    scopus 로고
    • Heterogeneity of monoclonal antibodies
    • Liu, H., D. Faldu, C. Chumsae, and J. Sun. 2008. Heterogeneity of monoclonal antibodies. J. Pharm. Sci. 97(7):2426-2447.
    • (2008) J. Pharm. Sci , vol.97 , Issue.7 , pp. 2426-2447
    • Liu, H.1    Faldu, D.2    Chumsae, C.3    Sun, J.4
  • 22
    • 34047270107 scopus 로고    scopus 로고
    • A role for protein misfolding in immunogenicity of biopharmaceuticals
    • Maas, C., et al. 2007. A role for protein misfolding in immunogenicity of biopharmaceuticals. J. Biol. Chem 282(4):2229-2236.
    • (2007) J. Biol. Chem , vol.282 , Issue.4 , pp. 2229-2236
    • Maas, C.1
  • 23
    • 84891018017 scopus 로고    scopus 로고
    • The continuing role of amino acid analysis in a biotechnology laboratory
    • In Amino Acid Analysis Protocols, ed. C. Cooper, N. Packer, and K. Williams, 9-30., no. 159. Totowa, NJ: Humana Press.
    • Macchi, F.D., F.J. Shen, R.G. Keck, and R.J. Harris. 2001. The continuing role of amino acid analysis in a biotechnology laboratory. In Amino Acid Analysis Protocols, ed. C. Cooper, N. Packer, and K. Williams, 9-30. Methods in Molecular Biology no. 159. Totowa, NJ: Humana Press.
    • (2001) Methods in Molecular Biology
    • Macchi, F.D.1    Shen, F.J.2    Keck, R.G.3    Harris, R.J.4
  • 24
    • 25444513733 scopus 로고    scopus 로고
    • Enhanced sensitivity and precision in an enzyme-linked immunosorbent assay with fluorogenic substrates compared with commonly used chromogenic substrates
    • Meng, Y., K. High, J. Antonello, M. Washabaugh, and Q. Zhao. 2005. Enhanced sensitivity and precision in an enzyme-linked immunosorbent assay with fluorogenic substrates compared with commonly used chromogenic substrates. Anal. Biochem. 345:227-236.
    • (2005) Anal. Biochem , vol.345 , pp. 227-236
    • Meng, Y.1    High, K.2    Antonello, J.3    Washabaugh, M.4    Zhao, Q.5
  • 25
    • 1242317024 scopus 로고    scopus 로고
    • Fucose depletion from human IgG1 oligosaccharide enhances binding enthalpy and association rate between IgG1 and FcgammaRIIIa
    • Okazaki, A., E. Shoji-Hosaka, K. Nakamura, et al. 2004. Fucose depletion from human IgG1 oligosaccharide enhances binding enthalpy and association rate between IgG1 and FcgammaRIIIa. J. Mol. Biol. 336(5): 1239-1249.
    • (2004) J. Mol. Biol , vol.336 , Issue.5 , pp. 1239-1249
    • Okazaki, A.1    Shoji-Hosaka, E.2    Nakamura, K.3
  • 26
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C.N., et al. 1995. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4(11):2411-2423.
    • (1995) Protein Sci , vol.4 , Issue.11 , pp. 2411-2423
    • Pace, C.N.1
  • 27
    • 0031799347 scopus 로고    scopus 로고
    • A high-throughput microscale method to release N-linked oligosaccharides from glycoproteins for matrix-assisted laser desorption/ionization time-of-flight mass spectro-metric analysis
    • Papac, D.I., J.B. Briggs, E.T. Chin, and A.J. Jones. 1998. A high-throughput microscale method to release N-linked oligosaccharides from glycoproteins for matrix-assisted laser desorption/ionization time-of-flight mass spectro-metric analysis. Glycobiology 8(5):445-454.
    • (1998) Glycobiology , vol.8 , Issue.5 , pp. 445-454
    • Papac, D.I.1    Briggs, J.B.2    Chin, E.T.3    Jones, A.J.4
  • 28
    • 0027791511 scopus 로고
    • Orthoclone OKT3. Chemical mechanisms and functional effects of degradation of a therapeutic antibody
    • In, ed. Y.J. Wang and R. Pearlman,, New York: Plenum Press.
    • Rao, P.E., and D.J. Kroon. 1993. Orthoclone OKT3. Chemical mechanisms and functional effects of degradation of a therapeutic antibody. In Stability and Characterization of Protein and Peptide Drugs: Case Histories, ed. Y.J. Wang and R. Pearlman, 135-158. New York: Plenum Press.
    • (1993) Stability and Characterization of Protein and Peptide Drugs: Case Histories , pp. 135-158
    • Rao, P.E.1    Kroon, D.J.2
  • 29
    • 0018416496 scopus 로고
    • Ellman's reagent: 5,5'-dithiobis(2-nitrobenzoic acid): A reex-amination
    • Riddles, P.W., R.L. Blakely, and B. Zerner. 1979. Ellman's reagent: 5,5'-dithiobis(2-nitrobenzoic acid): A reex-amination. Anal. Biochem. 94:75-81.
    • (1979) Anal. Biochem , vol.94 , pp. 75-81
    • Riddles, P.W.1    Blakely, R.L.2    Zerner, B.3
  • 30
    • 0024801675 scopus 로고
    • Antibody-dependent cytotoxicity mediated by natural killer cells is enhanced by castanospermine-induced alterations of IgG glycosylation
    • Rothman, R.J., B. Perussia, D. Herlyn, and L. Warren. 1989. Antibody-dependent cytotoxicity mediated by natural killer cells is enhanced by castanospermine-induced alterations of IgG glycosylation. Mol. Immunol. 26(12):1113-1123.
    • (1989) Mol. Immunol , vol.26 , Issue.12 , pp. 1113-1123
    • Rothman, R.J.1    Perussia, B.2    Herlyn, D.3    Warren, L.4
  • 31
    • 77957062488 scopus 로고    scopus 로고
    • The application of tert-butylhydroperoxide oxidation to study sites of potential methionine oxidation in a recombinant antibody
    • In, ed. D. Marshak,, San Diego: Academic Press.
    • Shen, F.J., M.Y. Kwong, R.G. Keck, and R.J. Harris. 1996. The application of tert-butylhydroperoxide oxidation to study sites of potential methionine oxidation in a recombinant antibody. In Techniques in Protein Chemistry, vol. 7, ed. D. Marshak, 275-284. San Diego: Academic Press.
    • (1996) Techniques in Protein Chemistry , vol.7 , pp. 275-284
    • Shen, F.J.1    Kwong, M.Y.2    Keck, R.G.3    Harris, R.J.4
  • 32
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity
    • Shields, R.L., J. Lai, R. Keck, et al. 2002. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J. Biol. Chem. 277(30):26733-26740.
    • (2002) J. Biol. Chem , vol.277 , Issue.30 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3
  • 33
    • 34248545257 scopus 로고    scopus 로고
    • Applications of mass spectrometry for the structural characterization of recombinant protein pharmaceuticals
    • Srebalus Barnes, C.A., and A. Lim. 2007. Applications of mass spectrometry for the structural characterization of recombinant protein pharmaceuticals. Mass Spectrometry Rev. 26(3):370-388.
    • (2007) Mass Spectrometry Rev , vol.26 , Issue.3 , pp. 370-388
    • Srebalus Barnes, C.A.1    Lim, A.2
  • 34
    • 0022003140 scopus 로고
    • Deglycosylation of asparagine-linked glycans by peptide: N-glycosidase F
    • Tarentino, A.L., C.M. Gomez, and T.H. Plummer, Jr. 1985. Deglycosylation of asparagine-linked glycans by peptide: N-glycosidase F. Biochemistry 24(17):4665-4671.
    • (1985) Biochemistry , vol.24 , Issue.17 , pp. 4665-4671
    • Tarentino, A.L.1    Gomez, C.M.2    Plummer Jr., T.H.3
  • 36
    • 0033585877 scopus 로고    scopus 로고
    • Variant antibody identification by peptide mapping
    • Wan, M., F.Y. Shiau, W. Gordon, and G. Wang. 1999. Variant antibody identification by peptide mapping. Biotechnol. Bioeng. 62:485-488.
    • (1999) Biotechnol. Bioeng , vol.62 , pp. 485-488
    • Wan, M.1    Shiau, F.Y.2    Gordon, W.3    Wang, G.4
  • 37
    • 0028566966 scopus 로고
    • Analysis of carbohydrates on IgG preparations
    • Weitzhandler, M., M. Hardy, M.S. Co, and N. Avdalovic. 1994. Analysis of carbohydrates on IgG preparations. J. Pharm. Sci. 83(12):1670-1675.
    • (1994) J. Pharm. Sci , vol.83 , Issue.12 , pp. 1670-1675
    • Weitzhandler, M.1    Hardy, M.2    Co, M.S.3    Avdalovic, N.4
  • 38
    • 84891021356 scopus 로고    scopus 로고
    • Evaluating the Disulfide Map of a Recombinant Membrane Protein by LC/MS/MS
    • (54th ASMS Conference on Mass Spectrometry and Allied Topics, Seattle, WA.)
    • Wenger, M., P. DePhillips, and L. Chen. 2006. Evaluating the Disulfide Map of a Recombinant Membrane Protein by LC/MS/MS. (54th ASMS Conference on Mass Spectrometry and Allied Topics, Seattle, WA.)
    • (2006)
    • Wenger, M.1    DePhillips, P.2    Chen, L.3
  • 39
    • 0031033895 scopus 로고    scopus 로고
    • Effect of glycosylation on antibody function: Implications for genetic engineering
    • Wright, A., and S.L. Morrison. 1997. Effect of glycosylation on antibody function: Implications for genetic engineering. Trends Biotechnol. 15(1):26-32.
    • (1997) Trends Biotechnol , vol.15 , Issue.1 , pp. 26-32
    • Wright, A.1    Morrison, S.L.2
  • 40
    • 0035988060 scopus 로고    scopus 로고
    • Free sulfhydryl in recombinant monoclonal antibodies
    • Zhang, W., and M.J. Czupryn. 2002. Free sulfhydryl in recombinant monoclonal antibodies. Biotechnol. Prog. 18:509-513.
    • (2002) Biotechnol. Prog , vol.18 , pp. 509-513
    • Zhang, W.1    Czupryn, M.J.2
  • 41
    • 0036901746 scopus 로고    scopus 로고
    • Complete disulfide bond assignment of a recombinant immunoglobulin G4 monoclonal antibody
    • Zhang, W., L.A. Marzilli, J.C. Rouse, and M.J. Czupryn. 2002. Complete disulfide bond assignment of a recombinant immunoglobulin G4 monoclonal antibody. Anal. Biochem. 311(1):1-9.
    • (2002) Anal. Biochem , vol.311 , Issue.1 , pp. 1-9
    • Zhang, W.1    Marzilli, L.A.2    Rouse, J.C.3    Czupryn, M.J.4


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