메뉴 건너뛰기




Volumn 29, Issue 1, 2012, Pages 187-197

Characterization of the isomerization products of aspartate residues at two different sites in a monoclonal antibody

Author keywords

Aspartic acid; Higher order structure; Isomerization; Monoclonal antibodies; Shelf life

Indexed keywords

ASPARTIC ACID; BUFFER; IMIDE; IMMUNOGLOBULIN G1 ANTIBODY; MONOCLONAL ANTIBODY; CARBOXYPEPTIDASE B; IMMUNOGLOBULIN G; ISOASPARTIC ACID; PAPAIN; PEPTIDE FRAGMENT;

EID: 84860567341     PISSN: 07248741     EISSN: 1573904X     Source Type: Journal    
DOI: 10.1007/s11095-011-0534-2     Document Type: Article
Times cited : (52)

References (30)
  • 1
    • 60849102492 scopus 로고    scopus 로고
    • Heterogeneity of monoclonal antibodies revealed by charge-sensitive methods
    • Vlasak J, Ionescu R. Heterogeneity of monoclonal antibodies revealed by charge-sensitive methods. Curr Pharm Biotechnol. 2008;9:468-81.
    • (2008) Curr Pharm Biotechnol , vol.9 , pp. 468-481
    • Vlasak, J.1    Ionescu, R.2
  • 2
    • 24944512327 scopus 로고    scopus 로고
    • Identification and characterization of deamidation sites in the conserved regions of human immunoglobulin gamma antibodies
    • DOI 10.1021/ac050672d
    • Chelius D, Rehder DS, Bondarenko PV. Identification and characterization of deamidation sites in the conserved regions of human Immunoglobulin Gamma antibodies. Anal Chem. 2005; 77:6004-11. (Pubitemid 41324303)
    • (2005) Analytical Chemistry , vol.77 , Issue.18 , pp. 6004-6011
    • Chelius, D.1    Render, D.S.2    Bondarenko, P.V.3
  • 3
    • 0030724407 scopus 로고    scopus 로고
    • Antioxidants for prevention of methionine oxidation in recombinant monoclonal antibody HER2
    • DOI 10.1021/js970143s
    • Lam XM, Yang JY, Cleland JL. Antioxidants for prevention of methionine oxidation in recombinant monoclonal antibody HER2. J Pharm Sci. 1997;86:1250-5. (Pubitemid 27486096)
    • (1997) Journal of Pharmaceutical Sciences , vol.86 , Issue.11 , pp. 1250-1255
    • Lam, X.M.1    Yang, J.Y.2    Cleland, J.L.3
  • 4
    • 27644506040 scopus 로고    scopus 로고
    • Studies on the mechanism of aspartic acid cleavage and glutamine deamidation in the acidic degradation of glucagon
    • DOI 10.1002/jps.20405
    • Joshi AB, Sawai M, Kearney WR, Kirsch LE. Studies on the mechanism of aspartic acid cleavage and glutamine deamidation in the acidic degradation of glucagon. J Pharm Sci. 2005;94:1912-27. (Pubitemid 41551476)
    • (2005) Journal of Pharmaceutical Sciences , vol.94 , Issue.9 , pp. 1912-1927
    • Joshi, A.B.1    Sawai, M.2    Kearney, W.R.3    Kirsch, L.E.4
  • 5
    • 0033755938 scopus 로고    scopus 로고
    • Determination of the origin of charge heterogeneity in a murine monoclonal antibody
    • Perkins M, Theiler R, Lunte S, Jeschke M. Determination of the origin of charge heterogeneity in a murine monoclonal antibody. Pharm Res. 2000;17:1110-7.
    • (2000) Pharm Res , vol.17 , pp. 1110-1117
    • Perkins, M.1    Theiler, R.2    Lunte, S.3    Jeschke, M.4
  • 6
    • 51549100828 scopus 로고    scopus 로고
    • Structural investigation of a phosphorylation-catalyzed, isoaspartate-free, protein succinimide: Crystallographic structure of post-succinimide His15Asp histidine-containing protein
    • Napper S, Prasad L, Delbaere LTJ. Structural investigation of a phosphorylation-catalyzed, isoaspartate-free, protein succinimide: crystallographic structure of post-succinimide His15Asp histidine-containing protein. Biochemistry. 2008;47:9486-96.
    • (2008) Biochemistry , vol.47 , pp. 9486-9496
    • Napper, S.1    Prasad, L.2    Delbaere, L.T.J.3
  • 7
    • 34447307909 scopus 로고    scopus 로고
    • 18O
    • DOI 10.1016/j.ab.2007.05.012, PII S0003269707003120
    • Terashima I, Koga A, Nagai H. Identification of deamidation and isomerization sites on pharmaceutical recombinant antibody using (H2O)-O-18. Anal Biochem. 2007;368:49-60. (Pubitemid 47058431)
    • (2007) Analytical Biochemistry , vol.368 , Issue.1 , pp. 49-60
    • Terashima, I.1    Koga, A.2    Nagai, H.3
  • 8
    • 34247108057 scopus 로고    scopus 로고
    • 18O labeling method for identification and quantification of succinimide in proteins
    • DOI 10.1021/ac0617870
    • Xiao G, Bondarenko PV, Jacob J, Chu GC, Chelius D. O-18 labeling method for identification and quantification of succinimide in proteins. Anal Chem. 2007;79:2714-21. (Pubitemid 46595624)
    • (2007) Analytical Chemistry , vol.79 , Issue.7 , pp. 2714-2721
    • Xiao, G.1    Bondarenko, P.V.2    Jacob, J.3    Chu, G.C.4    Chelius, D.5
  • 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. 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. 1996;35:1897-903.
    • (1996) Biochemistry , vol.35 , pp. 1897-1903
    • Cacia, J.1    Keck, R.2    Presta, L.G.3    Frenz, J.4
  • 10
    • 33750955290 scopus 로고    scopus 로고
    • Formulation considerations for proteins susceptible to asparagine deamidation and aspartate isomerization
    • DOI 10.1002/jps.20740
    • Wakankar AA, Borchardt RT. Formulation considerations for proteins susceptible to asparagine deamidation and aspartate isomerization. J Pharm Sci. 2006;95:2321-36. (Pubitemid 44732136)
    • (2006) Journal of Pharmaceutical Sciences , vol.95 , Issue.11 , pp. 2321-2336
    • Wakankar, A.A.1    Borchardt, R.T.2
  • 11
    • 0028260569 scopus 로고
    • Chemical pathways of peptide degradation. VI. Effect of the primary sequence on the pathways of degradation of aspartyl residues in model hexapeptides
    • DOI 10.1023/A:1018944800691
    • Oliyai C, Borchardt RT. Chemical pathways of peptide degradation .6. Effect of the primary sequence on the pathways of degradation of aspartyl residues in model hexapeptides. Pharm Res. 1994;11:751-8. (Pubitemid 24171774)
    • (1994) Pharmaceutical Research , vol.11 , Issue.5 , pp. 751-758
    • Oliyai, C.1    Borchardt, R.T.2
  • 13
    • 41549106299 scopus 로고    scopus 로고
    • Identification and quantification of degradations in the Asp-Asp motifs of a recombinant monoclonal antibody
    • Xiao G, Bondarenko PV. Identification and quantification of degradations in the Asp-Asp motifs of a recombinant monoclonal antibody. J Pharm Biomed Anal. 2008;47:23-30.
    • (2008) J Pharm Biomed Anal , vol.47 , pp. 23-30
    • Xiao, G.1    Bondarenko, P.V.2
  • 14
    • 34249059679 scopus 로고    scopus 로고
    • Accumulation of succinimide in a recombinant monoclonal antibody in mildly acidic buffers under elevated temperatures
    • DOI 10.1007/s11095-007-9241-4
    • Chu GC, Chelius D, Xiao G, Khor HK, Coulibaly S, Bondarenko PV. Accumulation of succinimide in a recombinant monoclonal antibody in mildly acidic buffers under elevated temperatures. Pharm Res. 2007;24:1145-56. (Pubitemid 46798894)
    • (2007) Pharmaceutical Research , vol.24 , Issue.6 , pp. 1145-1156
    • Chu, G.C.1    Chelius, D.2    Xiao, G.3    Khor, H.K.4    Coulibaly, S.5    Bondarenko, P.V.6
  • 15
    • 0029075220 scopus 로고
    • Effect of adjacent histidine and cysteine residues on the spontaneous degradation of asparaginyl-containing and aspartyl-containing peptides
    • Brennan TV, Clarke S. Effect of adjacent histidine and cysteine residues on the spontaneous degradation of asparaginyl-containing and aspartyl-containing peptides. Int J Pept Protein Res. 1995;45:547-53.
    • (1995) Int J Pept Protein Res , vol.45 , pp. 547-553
    • Brennan, T.V.1    Clarke, S.2
  • 16
    • 0027463564 scopus 로고
    • Chemical pathways of peptide degradation. IV. Pathways, kinetics, and mechanism of degradation of an aspartyl residue in a model hexapeptide
    • DOI 10.1023/A:1018981231468
    • Oliyai C, Borchardt RT. Chemical pathways of peptide degradation .4. Pathways, kinetics, and mechanism of degradation of an aspartyl residue in a model hexapeptide. Pharm Res. 1993;10:95-102. (Pubitemid 23020844)
    • (1993) Pharmaceutical Research , vol.10 , Issue.1 , pp. 95-102
    • Oliyai, C.1    Borchardt, R.T.2
  • 17
    • 33846967443 scopus 로고    scopus 로고
    • Aspartate isomerization in the complementarity-determining regions of two closely related monoclonal antibodies
    • Wakankar AA, Borchardt RT, Eigenbrot C, Shia S, Wang YJ, Shire SJ, et al. Aspartate isomerization in the complementarity-determining regions of two closely related monoclonal antibodies. Biochemistry. 2007;46:1534-44.
    • (2007) Biochemistry , vol.46 , pp. 1534-1544
    • Wakankar, A.A.1    Borchardt, R.T.2    Eigenbrot, C.3    Shia, S.4    Wang, Y.J.5    Shire, S.J.6
  • 19
    • 67749109890 scopus 로고    scopus 로고
    • Effect of protein structure on deamidation rate in the Fc fragment of an IgG1 monoclonal antibody
    • Sinha S, Zhang L, Duan SF, Williams TD, Vlasak J, Ionescu R, et al. Effect of protein structure on deamidation rate in the Fc fragment of an IgG1 monoclonal antibody. Protein Sci. 2009; 18:1573-84.
    • (2009) Protein Sci , vol.18 , pp. 1573-1584
    • Sinha, S.1    Zhang, L.2    Duan, S.F.3    Williams, T.D.4    Vlasak, J.5    Ionescu, R.6
  • 20
    • 0032904703 scopus 로고    scopus 로고
    • Secondary structure and protein deamidation
    • DOI 10.1021/js9802493
    • Xie M, Schowen RL. Secondary structure and protein deamidation. J Pharm Sci. 1999;88:8-13. (Pubitemid 29037362)
    • (1999) Journal of Pharmaceutical Sciences , vol.88 , Issue.1 , pp. 8-13
    • Xie, M.1    Schowen, R.L.2
  • 21
    • 0037163034 scopus 로고    scopus 로고
    • The influence of protein structure on the products emerging from succinimide hydrolysis
    • DOI 10.1074/jbc.M205314200
    • Athmer L, Kindrachuk J, Georges F, Napper S. The influence of protein structure on the products emerging from succinimide hydrolysis. J Biol Chem. 2002;277:30502-7. (Pubitemid 34970742)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.34 , pp. 30502-30507
    • Athmer, L.1    Kindrachuk, J.2    Georges, F.3    Napper, S.4
  • 22
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation
    • Geiger T, Clarke S. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides - succinimide-linked reactions that contribute to protein-degradation. J Biol Chem. 1987;262:785-94. (Pubitemid 17005254)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.2 , pp. 785-794
    • Geiger, T.1    Clarke, S.2
  • 23
    • 77951034970 scopus 로고    scopus 로고
    • Kinetics of chemical degradation in monoclonal antibodies: Relationship between rates at the molecular and peptide levels
    • Ionescu R, Vlasak J. Kinetics of chemical degradation in monoclonal antibodies: relationship between rates at the molecular and peptide levels. Anal Chem. 2010;82:3198-206.
    • (2010) Anal Chem , vol.82 , pp. 3198-3206
    • Ionescu, R.1    Vlasak, J.2
  • 24
    • 0033636448 scopus 로고    scopus 로고
    • Kinetic and thermodynamic control of the relative yield of the deamidation of asparagine and isomerization of aspartic acid residues
    • Capasso S, Di Cerbo P. Kinetic and thermodynamic control of the relative yield of the deamidation of asparagine and isomerization of aspartic acid residues. J Pept Res. 2000;56:382-7.
    • (2000) J Pept Res , vol.56 , pp. 382-387
    • Capasso, S.1    Di Cerbo, P.2
  • 30
    • 0028140248 scopus 로고
    • Deamidation and isoaspartate formation during in vitro aging of recombinant tissue plasminogen activator
    • Paranandi MV, Guzzetta AW, Hancock WS, Aswad DW. Deamidation and isoaspartate formation during in vitro aging of recombinant tissue plasminogen activator. J Biol Chem. 1994; 269:243-53. (Pubitemid 24026651)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.1 , pp. 243-253
    • Paranandi, M.V.1    Guzzetta, A.W.2    Hancock, W.S.3    Aswad, D.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.