메뉴 건너뛰기




Volumn 311, Issue 1, 2002, Pages 1-9

Complete disulfide bond assignment of a recombinant immunoglobulin G4 monoclonal antibody

Author keywords

Disulfide bond; Endoproteinase Lys C peptide map; Mass spectrometry; Monoclonal antibody; N terminal Edman sequencing; Reversed phase HPLC

Indexed keywords

COVALENT BONDS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; MONOCLONAL ANTIBODIES; PEPTIDES;

EID: 0036901746     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0003-2697(02)00394-9     Document Type: Article
Times cited : (79)

References (36)
  • 1
    • 0021719076 scopus 로고
    • Identification of the cystines which link the acidic and basic components of the glycinin subunits
    • P.E. Staswick, M.A. Hermodson, N.C. Nielsen, Identification of the cystines which link the acidic and basic components of the glycinin subunits, J. Biol. Chem. 259 (1984) 13431-13435.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13431-13435
    • Staswick, P.E.1    Hermodson, M.A.2    Nielsen, N.C.3
  • 2
    • 0022127514 scopus 로고
    • Peptide mapping of bovine pancreatic ribonuclease A by reverse-phase high-performance liquid chromatography. II. A two-dimensional technique for determination of disulfide pairings using a continuous-flow disulfide-detection system
    • T.W. Thannhauser, C.A. McWherter, H.A. Scheraga, Peptide mapping of bovine pancreatic ribonuclease A by reverse-phase high-performance liquid chromatography. II. A two-dimensional technique for determination of disulfide pairings using a continuous-flow disulfide-detection system, Anal. Biochem 149 (1985) 322-330.
    • (1985) Anal. Biochem. , vol.149 , pp. 322-330
    • Thannhauser, T.W.1    McWherter, C.A.2    Scheraga, H.A.3
  • 3
    • 0022087259 scopus 로고
    • Use of prolinespecific endopeptidase in the isolation of all four "native" disulfides of hen egg white lysozyme
    • L. Haeffner-Gormley, L. Parente, D.B. Wetlaufer, Use of prolinespecific endopeptidase in the isolation of all four "native" disulfides of hen egg white lysozyme, Int. J. Pept. Protein Res. 26 (1985) 83-91.
    • (1985) Int. J. Pept. Protein Res. , vol.26 , pp. 83-91
    • Haeffner-Gormley, L.1    Parente, L.2    Wetlaufer, D.B.3
  • 5
    • 0033863181 scopus 로고    scopus 로고
    • Characterization of cysteine residues and disulfide bonds in proteins by liquid chromatography/electrospray ionization tandem mass spectrometry
    • T.-Y. Yen, R.K. Joshi, H. Yan, N.O. Seto, M.M. Palcic, B.A. Macher, Characterization of cysteine residues and disulfide bonds in proteins by liquid chromatography/electrospray ionization tandem mass spectrometry, J. Mass Spectrom. 35 (2000) 990-1002.
    • (2000) J. Mass Spectrom. , vol.35 , pp. 990-1002
    • Yen, T.-Y.1    Joshi, R.K.2    Yan, H.3    Seto, N.O.4    Palcic, M.M.5    Macher, B.A.6
  • 6
    • 0026561566 scopus 로고
    • Characterization of disulfide bond position in proteins and sequence analysis of cystine-bridged peptides by tandem mass spectrometry
    • M.F. Bean, S.A. Carr, Characterization of disulfide bond position in proteins and sequence analysis of cystine-bridged peptides by tandem mass spectrometry, Anal. Biochem. 201 (1992) 216-226.
    • (1992) Anal. Biochem. , vol.201 , pp. 216-226
    • Bean, M.F.1    Carr, S.A.2
  • 7
    • 0031765415 scopus 로고    scopus 로고
    • Distinction between the three disulfide isomers of guanylin 99-115 by low-energy collision-induced dissociation
    • V. Badock, M. Raida, K. Adermann, W.-G. Forssmann, M. Schrader, Distinction between the three disulfide isomers of guanylin 99-115 by low-energy collision-induced dissociation, Rapid Commun. Mass Spectrom. 12 (1998) 1952-1956.
    • (1998) Rapid Commun. Mass Spectrom. , vol.12 , pp. 1952-1956
    • Badock, V.1    Raida, M.2    Adermann, K.3    Forssmann, W.-G.4    Schrader, M.5
  • 8
    • 0033548567 scopus 로고    scopus 로고
    • Disulfide bond structure and N-glycosylation sites of the extracellular domain of the human interleukin-6 receptor
    • A.R. Cole, N.E. Hall, H.R. Treutlein, J.S. Eddes, G.E. Reid, R.L. Moritz, R.J. Simpson, Disulfide bond structure and N-glycosylation sites of the extracellular domain of the human interleukin-6 receptor, J. Biol. Chem. 274 (1999) 7207-7215.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7207-7215
    • Cole, A.R.1    Hall, N.E.2    Treutlein, H.R.3    Eddes, J.S.4    Reid, G.E.5    Moritz, R.L.6    Simpson, R.J.7
  • 9
    • 0028544044 scopus 로고
    • Prompt fragmentation of disulfide-linked peptides during matrix-assisted laser desorption ionization mass spectrometry
    • S.D. Patterson, V. Katta, Prompt fragmentation of disulfide-linked peptides during matrix-assisted laser desorption ionization mass spectrometry, Anal. Chem. 66 (1994) 3727-3732.
    • (1994) Anal. Chem. , vol.66 , pp. 3727-3732
    • Patterson, S.D.1    Katta, V.2
  • 10
    • 0028906033 scopus 로고
    • Facile, in situ matrix-assisted laser desorption ionization-mass spectrometry analysis and assignment of disulfide pairings in heteropeptide molecules
    • D.L. Crimmins, M. Saylor, J. Rush, R.S. Thoma, Facile, in situ matrix-assisted laser desorption ionization-mass spectrometry analysis and assignment of disulfide pairings in heteropeptide molecules, Anal. Biochem. 226 (1995) 355-361.
    • (1995) Anal. Biochem. , vol.226 , pp. 355-361
    • Crimmins, D.L.1    Saylor, M.2    Rush, J.3    Thoma, R.S.4
  • 11
    • 0031601775 scopus 로고    scopus 로고
    • Determination of disulfide bonds in highly bridged disulfide-linked peptides by matrix-assisted laser desorption/ionization mass spectrometry with post-source decay
    • M.D. Jones, S.D. Patterson, H.S. Lu, Determination of disulfide bonds in highly bridged disulfide-linked peptides by matrix-assisted laser desorption/ionization mass spectrometry with post-source decay, Anal. Chem. 70 (1998) 136-143.
    • (1998) Anal. Chem. , vol.70 , pp. 136-143
    • Jones, M.D.1    Patterson, S.D.2    Lu, H.S.3
  • 12
    • 0031008622 scopus 로고    scopus 로고
    • Determination of the disulfide bond arrangement of human respiratory syncytial virus attachment (G) protein by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • J.J. Gorman, B.L. Ferguson, D. Speelman, J. Mills, Determination of the disulfide bond arrangement of human respiratory syncytial virus attachment (G) protein by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, Protein Sci. 6 (1997) 1308-1315.
    • (1997) Protein Sci. , vol.6 , pp. 1308-1315
    • Gorman, J.J.1    Ferguson, B.L.2    Speelman, D.3    Mills, J.4
  • 13
    • 0014887283 scopus 로고
    • Molecular size and conformation of immunoglobulins
    • K.J. Dorington, C. Tanford, Molecular size and conformation of immunoglobulins, Adv. Immunol. 12 (1970) 333-381.
    • (1970) Adv. Immunol. , vol.12 , pp. 333-381
    • Dorington, K.J.1    Tanford, C.2
  • 14
    • 0018253475 scopus 로고
    • The structural basis for the functional versatility of immunoglobulin G
    • K.J. Dorrington, The structural basis for the functional versatility of immunoglobulin G, Can. J. Biochem. 56 (1978) 1087-1101.
    • (1978) Can. J. Biochem. , vol.56 , pp. 1087-1101
    • Dorrington, K.J.1
  • 15
    • 0021857415 scopus 로고
    • Immunoglobulin G: Functional sites
    • D.R. Burton, Immunoglobulin G: Functional sites, Mol. Immunol. 22 (1985) 161-206.
    • (1985) Mol. Immunol. , vol.22 , pp. 161-206
    • Burton, D.R.1
  • 16
    • 0032763687 scopus 로고    scopus 로고
    • Strategies for locating disulfide bonds in a monoclonal antibody via mass spectrometry
    • R. Mhatre, J. Woodard, C. Zeng, Strategies for locating disulfide bonds in a monoclonal antibody via mass spectrometry, Rapid Commun. Mass Spectrom. 13 (1999) 2503-2510.
    • (1999) Rapid Commun. Mass Spectrom. , vol.13 , pp. 2503-2510
    • Mhatre, R.1    Woodard, J.2    Zeng, C.3
  • 17
    • 0036161645 scopus 로고    scopus 로고
    • Characterizing closely spaced, complex disulfide bond patterns in peptides and proteins by liquid chromatography/electrospray ionization tandem mass spectrometry
    • T.-Y. Yen, H. Yan, B.A. Macher, Characterizing closely spaced, complex disulfide bond patterns in peptides and proteins by liquid chromatography/electrospray ionization tandem mass spectrometry, J. Mass. Spectrom. 37 (2002) 15-30.
    • (2002) J. Mass. Spectrom. , vol.37 , pp. 15-30
    • Yen, T.-Y.1    Yan, H.2    Macher, B.A.3
  • 20
    • 0031058617 scopus 로고    scopus 로고
    • Intrachain disulfide bond in the core hinge region of human IgG4
    • J.W. Bloom, M.S. Madanat, D. Marriott, T. Wong, S.Y. Chan, Intrachain disulfide bond in the core hinge region of human IgG4, Protein Sci. 6 (1997) 407-415.
    • (1997) Protein Sci. , vol.6 , pp. 407-415
    • Bloom, J.W.1    Madanat, M.S.2    Marriott, D.3    Wong, T.4    Chan, S.Y.5
  • 21
    • 0034905149 scopus 로고    scopus 로고
    • The interheavy chain disulfide bonds of IgG4 are in equilibrium with intra-chain disulfide bonds
    • J. Schuurman, G.J. Perdok, A.D. Gorter, R.C. Aalberse, The interheavy chain disulfide bonds of IgG4 are in equilibrium with intra-chain disulfide bonds, Mol. Immunol. 38 (2001) 1-8.
    • (2001) Mol. Immunol. , vol.38 , pp. 1-8
    • Schuurman, J.1    Perdok, G.J.2    Gorter, A.D.3    Aalberse, R.C.4
  • 22
    • 0029065402 scopus 로고
    • Thiol/disulfide exchange equilibria and disulfide bond stability
    • H.F. Gilbert, Thiol/disulfide exchange equilibria and disulfide bond stability, Methods Enzymol. 251 (1995) 8-28.
    • (1995) Methods Enzymol. , vol.251 , pp. 8-28
    • Gilbert, H.F.1
  • 23
    • 0035988060 scopus 로고    scopus 로고
    • Free sulfhydryl in recombinant monoclonal antibodies
    • W. Zhang, M.J. Czupryn, Free sulfhydryl in recombinant monoclonal antibodies, Biotechnol. Prog. 18 (2002) 509-513.
    • (2002) Biotechnol. Prog. , vol.18 , pp. 509-513
    • Zhang, W.1    Czupryn, M.J.2
  • 24
    • 0013770208 scopus 로고
    • Reactions of N-ethylmaleimide with peptides and amino acids
    • D.G. Smyth, Reactions of N-ethylmaleimide with peptides and amino acids, Biochem. J. 91 (1964) 589-595.
    • (1964) Biochem. J. , vol.91 , pp. 589-595
    • Smyth, D.G.1
  • 26
    • 0027441371 scopus 로고
    • Assignment of the inter- and intramolecular disulfide linkages in recombinant human macrophage colony stimulating factor using fast atom bombardment mass spectrometry
    • M.O. Glocker, B. Arbogast, M.L. Deinzer, Assignment of the inter- and intramolecular disulfide linkages in recombinant human macrophage colony stimulating factor using fast atom bombardment mass spectrometry, Biochemistry 32 (1993) 482-488.
    • (1993) Biochemistry , vol.32 , pp. 482-488
    • Glocker, M.O.1    Arbogast, B.2    Deinzer, M.L.3
  • 27
    • 0035878235 scopus 로고    scopus 로고
    • Charge-state-dependent sequence analysis of protonated ubiquitin ions via ion trap tandem mass spectrometry
    • G.E. Reid, J. Wu, P.A. Chrisman, J.M. Wells, S.A. McLuckey, Charge-state-dependent sequence analysis of protonated ubiquitin ions via ion trap tandem mass spectrometry, Anal. Chem. 73 (2001) 3274-3281.
    • (2001) Anal. Chem. , vol.73 , pp. 3274-3281
    • Reid, G.E.1    Wu, J.2    Chrisman, P.A.3    Wells, J.M.4    McLuckey, S.A.5
  • 28
    • 0027448780 scopus 로고
    • Disulfide structures of highly bridged peptides: A new strategy for analysis
    • W.R. Gray, Disulfide structures of highly bridged peptides: A new strategy for analysis, Protein Sci. 2 (1993) 1732-1748.
    • (1993) Protein Sci. , vol.2 , pp. 1732-1748
    • Gray, W.R.1
  • 29
    • 0031050298 scopus 로고    scopus 로고
    • A Novel methodology for assignment of disulfide bond pairings in proteins
    • J. Wu, J.T. Watson, A novel methodology for assignment of disulfide bond pairings in proteins, Protein Sci. 6 (1997) 391-398.
    • (1997) Protein Sci. , vol.6 , pp. 391-398
    • Wu, J.1    Watson, J.T.2
  • 31
    • 0023547917 scopus 로고
    • Isolation and characterization of human cDNA clones encoding the alpha and the alpha subunits of casein kinase II
    • T. Marti, J. Rösselet, K. Titani, K.A. Walsh, Isolation and characterization of human cDNA clones encoding the alpha and the alpha subunits of casein kinase II, Biochemistry 26 (1987) 8099-8109.
    • (1987) Biochemistry , vol.26 , pp. 8099-8109
    • Marti, T.1    Rösselet, J.2    Titani, K.3    Walsh, K.A.4
  • 32
    • 0004125932 scopus 로고    scopus 로고
    • US Department of Health and Human Services, Food and Drug Administration, Center for Biologics Evaluation and Research, February 28
    • Points to Consider in the Manufacture and Testing of Monoclonal Antibody Products for Human Use, US Department of Health and Human Services, Food and Drug Administration, Center for Biologics Evaluation and Research, February 28, 1997.
    • (1997) Points to Consider in the Manufacture and Testing of Monoclonal Antibody Products for Human Use
  • 35
    • 0027987422 scopus 로고
    • Aggregation pathway of recombinant human keratinocyte growth factor and its stabilization
    • B.-L. Chen, T. Arakawa, C.F. Morris, W.C. Kenney, C.M. Wells, C.G. Pitt, Aggregation pathway of recombinant human keratinocyte growth factor and its stabilization, Pharm. Res. 11 (1994) 1581-1587.
    • (1994) Pharm. Res. , vol.11 , pp. 1581-1587
    • Chen, B.-L.1    Arakawa, T.2    Morris, C.F.3    Kenney, W.C.4    Wells, C.M.5    Pitt, C.G.6
  • 36
    • 0030826511 scopus 로고    scopus 로고
    • Oxidation of human insulin-like growth factor I in formulation studies. 3. Factorial experiments of the effects of ferric ions, EDTA, and visible light on methionine oxidation and covalent aggregation in aqueous solution
    • J.R. Fransson, Oxidation of human insulin-like growth factor I in formulation studies. 3. Factorial experiments of the effects of ferric ions, EDTA, and visible light on methionine oxidation and covalent aggregation in aqueous solution, J. Pharm. Sci. 86 (1997) 1046-1050.
    • (1997) J. Pharm. Sci. , vol.86 , pp. 1046-1050
    • Fransson, J.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.