메뉴 건너뛰기




Volumn 436, Issue 1, 2013, Pages 10-12

Method to convert N-terminal glutamine to pyroglutamate for characterization of recombinant monoclonal antibodies

Author keywords

Glutamine; Glutaminyl peptide cyclotransferase; Monoclonal antibodies; Pyroglutamate

Indexed keywords

CHROMATOGRAPHIC ANALYSIS; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; MONOCLONAL ANTIBODIES; PEPTIDES;

EID: 84874397693     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2013.01.017     Document Type: Article
Times cited : (19)

References (21)
  • 1
    • 0031466912 scopus 로고    scopus 로고
    • Validation of an HPLC method for the analysis of the charge heterogeneity of the recombinant monoclonal antibody IDEC-C2B8 after papain digestion
    • K.G. Moorhouse, W. Nashabeh, J. Deveney, N.S. Bjork, M.G. Mulkerrin, and T. Ryskamp Validation of an HPLC method for the analysis of the charge heterogeneity of the recombinant monoclonal antibody IDEC-C2B8 after papain digestion J. Pharm. Biomed. Anal. 16 1997 593 603
    • (1997) J. Pharm. Biomed. Anal. , vol.16 , pp. 593-603
    • Moorhouse, K.G.1    Nashabeh, W.2    Deveney, J.3    Bjork, N.S.4    Mulkerrin, M.G.5    Ryskamp, T.6
  • 2
    • 71749117526 scopus 로고    scopus 로고
    • Studies in serum support rapid formation of disulfide bond between unpaired cysteine residues in the VH domain of an immunoglobulin G1 molecule
    • D. Ouellette, L. Alessandri, A. Chin, C. Grinnell, E. Tarcsa, C. Radziejewski, and I. Correia Studies in serum support rapid formation of disulfide bond between unpaired cysteine residues in the VH domain of an immunoglobulin G1 molecule Anal. Biochem. 397 2009 37 47
    • (2009) Anal. Biochem. , vol.397 , pp. 37-47
    • Ouellette, D.1    Alessandri, L.2    Chin, A.3    Grinnell, C.4    Tarcsa, E.5    Radziejewski, C.6    Correia, I.7
  • 3
    • 29144436001 scopus 로고    scopus 로고
    • Analysis of recombinant monoclonal antibody isoforms by electrospray ionization mass spectrometry as a strategy for streamlining characterization of recombinant monoclonal antibody charge heterogeneity
    • Y. Lyubarskaya, D. Houde, J. Woodard, D. Murphy, and R. Mhatre Analysis of recombinant monoclonal antibody isoforms by electrospray ionization mass spectrometry as a strategy for streamlining characterization of recombinant monoclonal antibody charge heterogeneity Anal. Biochem. 348 2006 24 39
    • (2006) Anal. Biochem. , vol.348 , pp. 24-39
    • Lyubarskaya, Y.1    Houde, D.2    Woodard, J.3    Murphy, D.4    Mhatre, R.5
  • 5
    • 33646398313 scopus 로고    scopus 로고
    • Improving mass accuracy of high performance liquid chromatography/ electrospray ionization time-of-flight mass spectrometry of intact antibodies
    • H.S. Gadgil, G.D. Pipes, T.M. Dillon, M.J. Treuheit, and P.V. Bondarenko 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
  • 6
    • 0028258349 scopus 로고
    • Characterization of humanized anti-TAC, an antibody directed against the interleukin 2 receptor, using electrospray ionization mass spectrometry by direct infusion, LC/MS, and MS/MS
    • D.A. Lewis, A.W. Guzzetta, W.S. Hancock, and M. Costello Characterization of humanized anti-TAC, an antibody directed against the interleukin 2 receptor, using electrospray ionization mass spectrometry by direct infusion, LC/MS, and MS/MS Anal. Chem. 66 1994 585 595
    • (1994) Anal. Chem. , vol.66 , pp. 585-595
    • Lewis, D.A.1    Guzzetta, A.W.2    Hancock, W.S.3    Costello, M.4
  • 7
    • 29044447751 scopus 로고    scopus 로고
    • Reversed-phase liquid chromatography/mass spectrometry analysis of reduced monoclonal antibodies in pharmaceutics
    • D.S. Rehder, T.M. Dillon, G.D. Pipes, and P.V. Bondarenko Reversed-phase liquid chromatography/mass spectrometry analysis of reduced monoclonal antibodies in pharmaceutics J. Chromatogr. A 1102 2006 164 175
    • (2006) J. Chromatogr. A , vol.1102 , pp. 164-175
    • Rehder, D.S.1    Dillon, T.M.2    Pipes, G.D.3    Bondarenko, P.V.4
  • 8
    • 34249777508 scopus 로고    scopus 로고
    • Determination of the origin of the N-terminal pyro-glutamate variation in monoclonal antibodies using model peptides
    • L.W. Dick Jr., C. Kim, D. Qiu, and K.C. Cheng Determination of the origin of the N-terminal pyro-glutamate variation in monoclonal antibodies using model peptides Biotechnol. Bioeng. 97 2007 544 553
    • (2007) Biotechnol. Bioeng. , vol.97 , pp. 544-553
    • Dick, Jr.L.W.1    Kim, C.2    Qiu, D.3    Cheng, K.C.4
  • 10
    • 77951789012 scopus 로고    scopus 로고
    • Characterization of antibody charge heterogeneity resolved by preparative immobilized pH gradients
    • C.D. Meert, L.J. Brady, A. Guo, and A. Balland Characterization of antibody charge heterogeneity resolved by preparative immobilized pH gradients Anal. Chem. 82 2010 3510 3518
    • (2010) Anal. Chem. , vol.82 , pp. 3510-3518
    • Meert, C.D.1    Brady, L.J.2    Guo, A.3    Balland, A.4
  • 12
    • 79958256412 scopus 로고    scopus 로고
    • Fast analysis of recombinant monoclonal antibodies using IdeS proteolytic digestion and electrospray mass spectrometry
    • G. Chevreux, N. Tilly, and N. Bihoreau Fast analysis of recombinant monoclonal antibodies using IdeS proteolytic digestion and electrospray mass spectrometry Anal. Biochem. 415 2011 212 214
    • (2011) Anal. Biochem. , vol.415 , pp. 212-214
    • Chevreux, G.1    Tilly, N.2    Bihoreau, N.3
  • 14
    • 0033231450 scopus 로고    scopus 로고
    • Characterization of recombinant human monoclonal tissue necrosis factor-α antibody using cation-exchange HPLC and capillary isoelectric focusing
    • L.C. Santora, I.S. Krull, and K. Grant Characterization of recombinant human monoclonal tissue necrosis factor-α antibody using cation-exchange HPLC and capillary isoelectric focusing Anal. Biochem. 275 1999 98 108
    • (1999) Anal. Biochem. , vol.275 , pp. 98-108
    • Santora, L.C.1    Krull, I.S.2    Grant, K.3
  • 15
    • 0033755938 scopus 로고    scopus 로고
    • Determination of the origin of charge heterogeneity in a murine monoclonal antibody
    • M. Perkins, R. Theiler, S. Lunte, and M. Jeschke Determination of the origin of charge heterogeneity in a murine monoclonal antibody Pharm. Res. 17 2000 1110 1117
    • (2000) Pharm. Res. , vol.17 , pp. 1110-1117
    • Perkins, M.1    Theiler, R.2    Lunte, S.3    Jeschke, M.4
  • 16
    • 33748929886 scopus 로고    scopus 로고
    • Characterization of maleuric acid derivatives on transgenic human monoclonal antibody due to post-secretional modifications in goat milk
    • L.C. Santora, K. Stanley, I.S. Krull, and K. Grant Characterization of maleuric acid derivatives on transgenic human monoclonal antibody due to post-secretional modifications in goat milk Biomed. Chromatogr. 20 2006 843 856
    • (2006) Biomed. Chromatogr. , vol.20 , pp. 843-856
    • Santora, L.C.1    Stanley, K.2    Krull, I.S.3    Grant, K.4
  • 17
    • 33744466598 scopus 로고    scopus 로고
    • Characterization of the stability of a fully human monoclonal IgG after prolonged incubation at elevated temperature
    • H. Liu, G. Gaza-Bulseco, and J. Sun Characterization of the stability of a fully human monoclonal IgG after prolonged incubation at elevated temperature J. Chromatogr. B 837 2006 35 43
    • (2006) J. Chromatogr. B , vol.837 , pp. 35-43
    • Liu, H.1    Gaza-Bulseco, G.2    Sun, J.3
  • 18
    • 0024155599 scopus 로고    scopus 로고
    • Sequence analyses of two neuropeptides of the AKH/RPCH family from the lubber grasshopper, Romalea microptera
    • G. Gade, C. Hilbich, K. Beyreuther, and K.L. Rinehart Sequence analyses of two neuropeptides of the AKH/RPCH family from the lubber grasshopper, Romalea microptera Peptides 9 1998 681 688
    • (1998) Peptides , vol.9 , pp. 681-688
    • Gade, G.1    Hilbich, C.2    Beyreuther, K.3    Rinehart, K.L.4
  • 20
    • 0032127765 scopus 로고    scopus 로고
    • High-yield deblocking of amino termini of recombinant immunoglobulins with pyroglutamate aminopeptidase
    • J. Mozdzanowski, J. Bongers, and K. Anumula High-yield deblocking of amino termini of recombinant immunoglobulins with pyroglutamate aminopeptidase Anal. Biochem. 260 1998 183 187
    • (1998) Anal. Biochem. , vol.260 , pp. 183-187
    • Mozdzanowski, J.1    Bongers, J.2    Anumula, K.3
  • 21
    • 50849124123 scopus 로고    scopus 로고
    • Glutaminyl cyclases from animals and plants: A case of functionally convergent protein evolution
    • S. Schilling, C. Wasternack, and H.U. Demuth Glutaminyl cyclases from animals and plants: a case of functionally convergent protein evolution Biol. Chem. 389 2008 983 991
    • (2008) Biol. Chem. , vol.389 , pp. 983-991
    • Schilling, S.1    Wasternack, C.2    Demuth, H.U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.