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Volumn 491, Issue , 2015, Pages 52-54

Characterization of monoclonal antibodies by a fast and easy liquid chromatography-mass spectrometry time-of-flight analysis on culture supernatant

Author keywords

Fucosylation; Glycoform; Mass spectrometry; Monoclonal antibody

Indexed keywords

CAPILLARY ELECTROPHORESIS; MASS SPECTROMETRY; MONOCLONAL ANTIBODIES;

EID: 84944050131     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2015.08.006     Document Type: Article
Times cited : (12)

References (11)
  • 1
    • 84920502297 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks 2014
    • G. Walsh Biopharmaceutical benchmarks 2014 Nat. Biotechnol. 32 2014 992 1000
    • (2014) Nat. Biotechnol. , vol.32 , pp. 992-1000
    • Walsh, G.1
  • 2
    • 84874616206 scopus 로고    scopus 로고
    • Protein digestion: An overview of the available techniques and recent developments
    • L. Switzar, M. Giera, and W.M. Niessen Protein digestion: an overview of the available techniques and recent developments J. Proteome Res. 12 2013 1067 1077
    • (2013) J. Proteome Res. , vol.12 , pp. 1067-1077
    • Switzar, L.1    Giera, M.2    Niessen, W.M.3
  • 3
    • 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
  • 4
    • 84896536985 scopus 로고    scopus 로고
    • Middle-down analysis of monoclonal antibodies with electron transfer dissociation orbitrap fourier transform mass spectrometry
    • L. Fornelli, D. Ayoub, K. Aizikov, A. Beck, and Y.O. Tsybin Middle-down analysis of monoclonal antibodies with electron transfer dissociation orbitrap fourier transform mass spectrometry Anal. Chem. 86 2014 3005 3012
    • (2014) Anal. Chem. , vol.86 , pp. 3005-3012
    • Fornelli, L.1    Ayoub, D.2    Aizikov, K.3    Beck, A.4    Tsybin, Y.O.5
  • 6
    • 82455171807 scopus 로고    scopus 로고
    • Rapid LC-MS screening for IgG Fc modifications and allelic variants in blood
    • A.M. Goetze, Z. Zhang, L. Liu, F.W. Jacobsen, and G.C. Flynn Rapid LC-MS screening for IgG Fc modifications and allelic variants in blood Mol. Immunol. 49 2011 338 352
    • (2011) Mol. Immunol. , vol.49 , pp. 338-352
    • Goetze, A.M.1    Zhang, Z.2    Liu, L.3    Jacobsen, F.W.4    Flynn, G.C.5
  • 7
    • 77953603827 scopus 로고    scopus 로고
    • Ranking the susceptibility of disulfide bonds in human IgG1 antibodies by reduction, differential alkylation, and LC-MS analysis
    • H. Liu, C. Chumsae, G. Gaza-Bulseco, K. Hurkmans, and C.H. Radziejewski Ranking the susceptibility of disulfide bonds in human IgG1 antibodies by reduction, differential alkylation, and LC-MS analysis Anal. Chem. 82 2010 5219 5226
    • (2010) Anal. Chem. , vol.82 , pp. 5219-5226
    • Liu, H.1    Chumsae, C.2    Gaza-Bulseco, G.3    Hurkmans, K.4    Radziejewski, C.H.5
  • 9
    • 0029879785 scopus 로고    scopus 로고
    • High-resolution carbohydrate profiling by capillary gel electrophoresis
    • A. Guttman High-resolution carbohydrate profiling by capillary gel electrophoresis Nature 380 1996 461 462
    • (1996) Nature , vol.380 , pp. 461-462
    • Guttman, A.1
  • 10
    • 79959926784 scopus 로고    scopus 로고
    • Rapid high-resolution characterization of functionally important monoclonal antibody N-glycans by capillary electrophoresis
    • Z. Szabo, A. Guttman, J. Bones, and B.L. Karger Rapid high-resolution characterization of functionally important monoclonal antibody N-glycans by capillary electrophoresis Anal. Chem. 83 2011 5329 5336
    • (2011) Anal. Chem. , vol.83 , pp. 5329-5336
    • Szabo, Z.1    Guttman, A.2    Bones, J.3    Karger, B.L.4
  • 11
    • 10644276295 scopus 로고    scopus 로고
    • Enzymatic characterization of the streptococcal endopeptidase, IdeS, reveals that it is a cysteine protease with strict specificity for IgG cleavage due to exosite binding
    • B. Vincents, U. von Pawel-Rammingen, L. Björck, and M. Abrahamson Enzymatic characterization of the streptococcal endopeptidase, IdeS, reveals that it is a cysteine protease with strict specificity for IgG cleavage due to exosite binding Biochemistry 43 2004 15540 15549
    • (2004) Biochemistry , vol.43 , pp. 15540-15549
    • Vincents, B.1    Von Pawel-Rammingen, U.2    Björck, L.3    Abrahamson, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.