메뉴 건너뛰기




Volumn 7, Issue 1, 2012, Pages

Simultaneous assessment of Asp isomerization and Asn deamidation in recombinant antibodies by LC-MS following incubation at elevated temperatures

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; ASPARTIC ACID; BIOLOGICAL MARKER; CHLORIDE; HISTIDINE; IMMUNOGLOBULIN G1 ANTIBODY; RECOMBINANT ANTIBODY; AMIDE; ANTIBODY; IMMUNOGLOBULIN G; RECOMBINANT PROTEIN;

EID: 84855860373     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0030295     Document Type: Article
Times cited : (105)

References (31)
  • 1
    • 77952812537 scopus 로고    scopus 로고
    • Mass spectrometric analysis of asparagine deamidation and aspartate isomerization in polypeptides
    • Yang H, Zubarev RA, (2010) Mass spectrometric analysis of asparagine deamidation and aspartate isomerization in polypeptides. Electrophoresis 31: 1764-1772.
    • (2010) Electrophoresis , vol.31 , pp. 1764-1772
    • Yang, H.1    Zubarev, R.A.2
  • 2
    • 60849102492 scopus 로고    scopus 로고
    • Heterogeneity of monoclonal antibodies revealed by charge-sensitive methods
    • Vlasak J, Ionescu R, (2008) Heterogeneity of monoclonal antibodies revealed by charge-sensitive methods. Curr Pharm Biotechnol 9: 468-481.
    • (2008) Curr Pharm Biotechnol , vol.9 , pp. 468-481
    • Vlasak, J.1    Ionescu, R.2
  • 3
    • 33750955290 scopus 로고    scopus 로고
    • Formulation considerations for proteins susceptible to asparagine deamidation and aspartate isomerization
    • Wakankar AA, Borchardt RT, (2006) Formulation considerations for proteins susceptible to asparagine deamidation and aspartate isomerization. J Pharm Sci 95: 2321-2336.
    • (2006) J Pharm Sci , vol.95 , pp. 2321-2336
    • Wakankar, A.A.1    Borchardt, R.T.2
  • 4
    • 24944532072 scopus 로고    scopus 로고
    • Biological significance of isoaspartate and its repair system
    • Shimizu T, Matsuoka Y, Shirasawa T, (2005) Biological significance of isoaspartate and its repair system. Biol Pharm Bull 28: 1590-1596.
    • (2005) Biol Pharm Bull , vol.28 , pp. 1590-1596
    • Shimizu, T.1    Matsuoka, Y.2    Shirasawa, T.3
  • 5
    • 0023682520 scopus 로고
    • Does the chemical instability of aspartyl and asparaginyl residues in proteins contribute to erythrocyte aging? The role of protein carboxyl methylation reactions
    • Lowenson J, Clarke S, (1988) Does the chemical instability of aspartyl and asparaginyl residues in proteins contribute to erythrocyte aging? The role of protein carboxyl methylation reactions. Blood Cells 14: 103-118.
    • (1988) Blood Cells , vol.14 , pp. 103-118
    • Lowenson, J.1    Clarke, S.2
  • 6
    • 33644619972 scopus 로고    scopus 로고
    • Heterogeneity of recombinant antibodies: linking structure to function
    • Harris RJ, (2005) Heterogeneity of recombinant antibodies: linking structure to function. Dev Biol (Basel) 122: 117-127.
    • (2005) Dev Biol (Basel) , vol.122 , pp. 117-127
    • Harris, R.J.1
  • 7
    • 0014408806 scopus 로고
    • Multiple forms of cytochrome c in the rat. Precursor-product relationship between the main component Cy I and the minor components Cy II and Cy 3 in vivo
    • Flatmark T, Sletten K, (1968) Multiple forms of cytochrome c in the rat. Precursor-product relationship between the main component Cy I and the minor components Cy II and Cy 3 in vivo. J Biol Chem 243: 1623-1629.
    • (1968) J Biol Chem , vol.243 , pp. 1623-1629
    • Flatmark, T.1    Sletten, K.2
  • 8
  • 9
    • 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, Keck R, Presta LG, Frenz J, (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
  • 10
    • 0028300715 scopus 로고
    • Chemical and physical stability of chimeric L6, a mouse-human monoclonal antibody
    • Paborji M, Pochopin NL, Coppola WP, Bogardus JB, (1994) Chemical and physical stability of chimeric L6, a mouse-human monoclonal antibody. Pharm Res 11: 764-771.
    • (1994) Pharm Res , vol.11 , pp. 764-771
    • Paborji, M.1    Pochopin, N.L.2    Coppola, W.P.3    Bogardus, J.B.4
  • 11
    • 0026463719 scopus 로고
    • Identification of sites of degradation in a therapeutic monoclonal antibody by peptide mapping
    • Kroon DJ, Baldwin-Ferro A, Lalan P, (1992) Identification of sites of degradation in a therapeutic monoclonal antibody by peptide mapping. Pharm Res 9: 1386-1393.
    • (1992) Pharm Res , vol.9 , pp. 1386-1393
    • Kroon, D.J.1    Baldwin-Ferro, A.2    Lalan, P.3
  • 13
    • 14744268457 scopus 로고    scopus 로고
    • In vivo deamidation characterization of monoclonal antibody by LC/MS/MS
    • Huang L, Lu J, Wroblewski VJ, Beals JM, Riggin RM, (2005) In vivo deamidation characterization of monoclonal antibody by LC/MS/MS. Anal Chem 77: 1432-1439.
    • (2005) Anal Chem , vol.77 , pp. 1432-1439
    • Huang, L.1    Lu, J.2    Wroblewski, V.J.3    Beals, J.M.4    Riggin, R.M.5
  • 14
    • 70349229289 scopus 로고    scopus 로고
    • Succinimide formation at Asn 55 in the complementarity determining region of a recombinant monoclonal antibody IgG1 heavy chain
    • Yan B, Steen S, Hambly D, Valliere-Douglass J, Vanden Bos T, et al. (2009) Succinimide formation at Asn 55 in the complementarity determining region of a recombinant monoclonal antibody IgG1 heavy chain. J Pharm Sci 98: 3509-3521.
    • (2009) J Pharm Sci , vol.98 , pp. 3509-3521
    • Yan, B.1    Steen, S.2    Hambly, D.3    Valliere-Douglass, J.4    van den Bos, T.5
  • 15
    • 34249059679 scopus 로고    scopus 로고
    • Accumulation of succinimide in a recombinant monoclonal antibody in mildly acidic buffers under elevated temperatures
    • Chu GC, Chelius D, Xiao G, Khor HK, Coulibaly S, et al. (2007) Accumulation of succinimide in a recombinant monoclonal antibody in mildly acidic buffers under elevated temperatures. Pharm Res 24: 1145-1156.
    • (2007) Pharm Res , vol.24 , pp. 1145-1156
    • Chu, G.C.1    Chelius, D.2    Xiao, G.3    Khor, H.K.4    Coulibaly, S.5
  • 16
    • 24944512327 scopus 로고    scopus 로고
    • Identification and characterization of deamidation sites in the conserved regions of human immunoglobulin gamma antibodies
    • Chelius D, Rehder DS, Bondarenko PV, (2005) Identification and characterization of deamidation sites in the conserved regions of human immunoglobulin gamma antibodies. Anal Chem 77: 6004-6011.
    • (2005) Anal Chem , vol.77 , pp. 6004-6011
    • Chelius, D.1    Rehder, D.S.2    Bondarenko, P.V.3
  • 17
    • 0023664602 scopus 로고
    • Methylation at specific altered aspartyl and asparaginyl residues in glucagon by the erythrocyte protein carboxyl methyltransferase
    • Ota IM, Ding L, Clarke S, (1987) Methylation at specific altered aspartyl and asparaginyl residues in glucagon by the erythrocyte protein carboxyl methyltransferase. J Biol Chem 262: 8522-8531.
    • (1987) J Biol Chem , vol.262 , pp. 8522-8531
    • Ota, I.M.1    Ding, L.2    Clarke, S.3
  • 18
    • 0027363478 scopus 로고
    • In vitro aging of calmodulin generates isoaspartate at multiple Asn-Gly and Asp-Gly sites in calcium-binding domains II, III, and IV
    • Potter SM, Henzel WJ, Aswad DW, (1993) In vitro aging of calmodulin generates isoaspartate at multiple Asn-Gly and Asp-Gly sites in calcium-binding domains II, III, and IV. Protein Sci 2: 1648-1663.
    • (1993) Protein Sci , vol.2 , pp. 1648-1663
    • Potter, S.M.1    Henzel, W.J.2    Aswad, D.W.3
  • 19
    • 0028180406 scopus 로고
    • Identification of succinimide sites in proteins by N-terminal sequence analysis after alkaline hydroxylamine cleavage
    • Kwong MY, Harris RJ, (1994) Identification of succinimide sites in proteins by N-terminal sequence analysis after alkaline hydroxylamine cleavage. Protein Sci 3: 147-149.
    • (1994) Protein Sci , vol.3 , pp. 147-149
    • Kwong, M.Y.1    Harris, R.J.2
  • 20
    • 0025740502 scopus 로고
    • Isolation and characterization of a succinimide variant of methionyl human growth hormone
    • Teshima G, Stults JT, Ling V, Canova-Davis E, (1991) Isolation and characterization of a succinimide variant of methionyl human growth hormone. J Biol Chem 266: 13544-13547.
    • (1991) J Biol Chem , vol.266 , pp. 13544-13547
    • Teshima, G.1    Stults, J.T.2    Ling, V.3    Canova-Davis, E.4
  • 21
    • 13244249515 scopus 로고    scopus 로고
    • Deamidation: Differentiation of aspartyl from isoaspartyl products in peptides by electron capture dissociation
    • Cournoyer JJ, Pittman JL, Ivleva VB, Fallows E, Waskell L, et al. (2005) Deamidation: Differentiation of aspartyl from isoaspartyl products in peptides by electron capture dissociation. Protein Sci 14: 452-463.
    • (2005) Protein Sci , vol.14 , pp. 452-463
    • Cournoyer, J.J.1    Pittman, J.L.2    Ivleva, V.B.3    Fallows, E.4    Waskell, L.5
  • 22
    • 0035894272 scopus 로고    scopus 로고
    • Broadband detection electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry to reveal enzymatically and chemically induced deamidation reactions within peptides
    • Schmid DG, von der Mulbe FD, Fleckenstein B, Weinschenk T, Jung G, (2001) Broadband detection electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry to reveal enzymatically and chemically induced deamidation reactions within peptides. Anal Chem 73: 6008-6013.
    • (2001) Anal Chem , vol.73 , pp. 6008-6013
    • Schmid, D.G.1    von der Mulbe, F.D.2    Fleckenstein, B.3    Weinschenk, T.4    Jung, G.5
  • 23
    • 31044442964 scopus 로고    scopus 로고
    • Stepwise deamidation of ribonuclease A at five sites determined by top down mass spectrometry
    • Zabrouskov V, Han X, Welker E, Zhai H, Lin C, et al. (2006) Stepwise deamidation of ribonuclease A at five sites determined by top down mass spectrometry. Biochemistry 45: 987-992.
    • (2006) Biochemistry , vol.45 , pp. 987-992
    • Zabrouskov, V.1    Han, X.2    Welker, E.3    Zhai, H.4    Lin, C.5
  • 24
    • 33845300569 scopus 로고    scopus 로고
    • Measurement of deamidation of intact proteins by isotopic envelope and mass defect with ion cyclotron resonance Fourier transform mass spectrometry
    • Robinson NE, Zabrouskov V, Zhang J, Lampi KJ, Robinson AB, (2006) Measurement of deamidation of intact proteins by isotopic envelope and mass defect with ion cyclotron resonance Fourier transform mass spectrometry. Rapid Commun Mass Spectrom 20: 3535-3541.
    • (2006) Rapid Commun Mass Spectrom , vol.20 , pp. 3535-3541
    • Robinson, N.E.1    Zabrouskov, V.2    Zhang, J.3    Lampi, K.J.4    Robinson, A.B.5
  • 25
    • 0026426005 scopus 로고
    • Integration of mass spectrometry in analytical biotechnology
    • Carr SA, Hemling ME, Bean MF, Roberts GD, (1991) Integration of mass spectrometry in analytical biotechnology. Anal Chem 63: 2802-2824.
    • (1991) Anal Chem , vol.63 , pp. 2802-2824
    • Carr, S.A.1    Hemling, M.E.2    Bean, M.F.3    Roberts, G.D.4
  • 26
    • 34247108057 scopus 로고    scopus 로고
    • 18O labeling method for identification and quantification of succinimide in proteins
    • Xiao G, Bondarenko PV, Jacob J, Chu GC, Chelius D, (2007) 18O labeling method for identification and quantification of succinimide in proteins. Anal Chem 79: 2714-2721.
    • (2007) Anal Chem , vol.79 , pp. 2714-2721
    • Xiao, G.1    Bondarenko, P.V.2    Jacob, J.3    Chu, G.C.4    Chelius, D.5
  • 27
    • 63649161438 scopus 로고    scopus 로고
    • Direct identification and quantification of aspartyl succinimide in an IgG2 mAb by RapiGest assisted digestion
    • Huang HZ, Nichols A, Liu D, (2009) Direct identification and quantification of aspartyl succinimide in an IgG2 mAb by RapiGest assisted digestion. Anal Chem 81: 1686-1692.
    • (2009) Anal Chem , vol.81 , pp. 1686-1692
    • Huang, H.Z.1    Nichols, A.2    Liu, D.3
  • 28
    • 77449103392 scopus 로고    scopus 로고
    • Identification and characterization of oxidation and deamidation sites in monoclonal rat/mouse hybrid antibodies
    • Timm V, Gruber P, Wasiliu M, Lindhofer H, Chelius D, (2010) Identification and characterization of oxidation and deamidation sites in monoclonal rat/mouse hybrid antibodies. J Chromatogr B Analyt Technol Biomed Life Sci 878: 777-784.
    • (2010) J Chromatogr B Analyt Technol Biomed Life Sci , vol.878 , pp. 777-784
    • Timm, V.1    Gruber, P.2    Wasiliu, M.3    Lindhofer, H.4    Chelius, D.5
  • 29
    • 79551550805 scopus 로고    scopus 로고
    • Identification of isomerization and racemization of aspartate in the Asp-Asp motifs of a therapeutic protein
    • Zhang J, Yip H, Katta V, (2011) Identification of isomerization and racemization of aspartate in the Asp-Asp motifs of a therapeutic protein. Anal Biochem 410: 234-243.
    • (2011) Anal Biochem , vol.410 , pp. 234-243
    • Zhang, J.1    Yip, H.2    Katta, V.3
  • 30
    • 79961009713 scopus 로고    scopus 로고
    • Accurate Determination of Succinimide Degradation Products Using High Fidelity Trypsin Digestion Peptide Map Analysis
    • Yu XC, Joe K, Zhang Y, Adriano A, Wang Y, et al. (2011) Accurate Determination of Succinimide Degradation Products Using High Fidelity Trypsin Digestion Peptide Map Analysis. Anal Chem 83: 5912-5919.
    • (2011) Anal Chem , vol.83 , pp. 5912-5919
    • Yu, X.C.1    Joe, K.2    Zhang, Y.3    Adriano, A.4    Wang, Y.5
  • 31
    • 79952291899 scopus 로고    scopus 로고
    • Identification of potential sites for tryptophan oxidation in recombinant antibodies using tert-butylhydroperoxide and quantitative LC-MS
    • Hensel M, Steurer R, Fichtl J, Elger C, Wedekind F, et al. (2011) Identification of potential sites for tryptophan oxidation in recombinant antibodies using tert-butylhydroperoxide and quantitative LC-MS. PLoS One 6: e17708.
    • (2011) PLoS One , vol.6
    • Hensel, M.1    Steurer, R.2    Fichtl, J.3    Elger, C.4    Wedekind, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.