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Volumn 105, Issue 1, 2010, Pages 121-129

Aggregation of a monoclonal antibody induced by adsorption to stainless steel

Author keywords

Adsorption; Kinetics; Mechanism; Monoclonal antibody; Protein aggregation; Stainless steel

Indexed keywords

ADSORBED LAYERS; ADSORPTION KINETICS; ADSORPTION LAYER; AGGREGATION PROCESS; BIOPHARMACEUTICAL PRODUCTS; BULK PHASE; CARBONYL GROUPS; INITIAL RATE; MASS SPECTRA; MICRO-PARTICLES; MONOCLONAL ANTIBODIES (MAB); POLYSORBATE 20; PROTEIN AGGREGATION; PROTEIN OXIDATION; RATE-LIMITING STEPS; SECOND ORDERS; STAINLESS STEEL SURFACE; STEEL SURFACE; SURFACE AGGREGATION; THERAPEUTIC PROTEIN; ZERO ORDER;

EID: 73949093277     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.22525     Document Type: Article
Times cited : (87)

References (23)
  • 1
    • 52449112053 scopus 로고    scopus 로고
    • High concentration formulations of recombinant human interleukin-1 receptor antagonist: II. Aggregation kinetics
    • Alford JR, Kendrick BS, Carpenter JF, Randolph TW. 2008. High concentration formulations of recombinant human interleukin-1 receptor antagonist: II. Aggregation kinetics. J Pharm Sci 97(8):3005-3021.
    • (2008) J Pharm Sci , vol.97 , Issue.8 , pp. 3005-3021
    • Alford, J.R.1    Kendrick, B.S.2    Carpenter, J.F.3    Randolph, T.W.4
  • 3
    • 68949119488 scopus 로고    scopus 로고
    • Monoclonal antibody interactions with micro-and nanoparticles: Adsorption, aggregation, and accelerated stress studies
    • Bee JS, Chiu D, Sawicki S, Stevenson JL, Chatterjee K, Freund E, Carpenter JF, Randolph TW. 2009. Monoclonal antibody interactions with micro-and nanoparticles: Adsorption, aggregation, and accelerated stress studies. J Pharm Sci 98(9):3218-3238.
    • (2009) J Pharm Sci , vol.98 , Issue.9 , pp. 3218-3238
    • Bee, J.S.1    Chiu, D.2    Sawicki, S.3    Stevenson, J.L.4    Chatterjee, K.5    Freund, E.6    Carpenter, J.F.7    Randolph, T.W.8
  • 4
    • 35348827271 scopus 로고    scopus 로고
    • Determining antibody stability: Creation of solid-liquid interfacial effects within a high shear environment
    • Biddlecombe JG, Craig AV, Zhang H, Uddin S, Mulot S, Fish BC, Bracewell DG. 2007. Determining antibody stability: Creation of solid-liquid interfacial effects within a high shear environment. Biotechnol Prog 23(5):1218-1222.
    • (2007) Biotechnol Prog , vol.23 , Issue.5 , pp. 1218-1222
    • Biddlecombe, J.G.1    Craig, A.V.2    Zhang, H.3    Uddin, S.4    Mulot, S.5    Fish, B.C.6    Bracewell, D.G.7
  • 5
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in non-native protein aggregation
    • Chi EY, Krishnan S, Randolph TW, Carpenter JF. 2003. Physical stability of proteins in aqueous solution: Mechanism and driving forces in non-native protein aggregation. Pharm Res 20(9):1325-1336.
    • (2003) Pharm Res , vol.20 , Issue.9 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 6
    • 0034771050 scopus 로고    scopus 로고
    • Comparison between light induced and chemically induced oxidation of rhVEGF
    • Duenas ET, Keck R, De Vos A, Jones AJS, Cleland JL. 2001. Comparison between light induced and chemically induced oxidation of rhVEGF. Pharm Res 18(10):1455-1460.
    • (2001) Pharm Res , vol.18 , Issue.10 , pp. 1455-1460
    • Duenas, E.T.1    Keck, R.2    De Vos, A.3    Jones, A.J.S.4    Cleland, J.L.5
  • 8
    • 0037150069 scopus 로고    scopus 로고
    • Relationship between protein structure and methionine oxidation in recombinant human alpha 1-antitrypsin
    • Griffiths SW, Cooney CL. 2002. Relationship between protein structure and methionine oxidation in recombinant human alpha 1-antitrypsin. Biochemistry 41(20):6245-6252.
    • (2002) Biochemistry , vol.41 , Issue.20 , pp. 6245-6252
    • Griffiths, S.W.1    Cooney, C.L.2
  • 9
    • 0030724407 scopus 로고    scopus 로고
    • Antioxidants for prevention of methionine oxidation in recombinant monoclonal antibody HER2
    • Lam XM, Yang JY, Cleland JL. 1997. Antioxidants for prevention of methionine oxidation in recombinant monoclonal antibody HER2. J Pharm Sci 86(11):1250-1255.
    • (1997) J Pharm Sci , vol.86 , Issue.11 , pp. 1250-1255
    • Lam, X.M.1    Yang, J.Y.2    Cleland, J.L.3
  • 11
    • 34848814407 scopus 로고    scopus 로고
    • Structural effect of deglycosylation and methionine oxidation on a recombinant monoclonal antibody
    • Liu HC, Gaza-Bulseco G, Xiang T, Chumsae C. 2008. Structural effect of deglycosylation and methionine oxidation on a recombinant monoclonal antibody. Mol Immunol 45(3):701-708.
    • (2008) Mol Immunol , vol.45 , Issue.3 , pp. 701-708
    • Liu, H.C.1    Gaza-Bulseco, G.2    Xiang, T.3    Chumsae, C.4
  • 12
    • 34547702184 scopus 로고    scopus 로고
    • Engineering challenges of protein formulations
    • Randolph TW, Carpenter JF. 2007. Engineering challenges of protein formulations. AIChE J 53(8):1902-1907.
    • (2007) AIChE J , vol.53 , Issue.8 , pp. 1902-1907
    • Randolph, T.W.1    Carpenter, J.F.2
  • 14
    • 36749040335 scopus 로고    scopus 로고
    • Non-native protein aggregation kinetics
    • Roberts CJ. 2007. Non-native protein aggregation kinetics. Biotechnol Bioeng 98(5):927-938.
    • (2007) Biotechnol Bioeng , vol.98 , Issue.5 , pp. 927-938
    • Roberts, C.J.1
  • 15
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: An immunologic perspective
    • Rosenberg AS. 2006. Effects of protein aggregates: An immunologic perspective. AAPS J 8(3):E501-E507.
    • (2006) AAPS , vol.J 8 , Issue.3
    • Rosenberg, A.S.1
  • 16
    • 0036861899 scopus 로고    scopus 로고
    • Immunogenicity of therapeutic proteins: Clinical implications and future prospects
    • Schellekens H. 2002. Immunogenicity of therapeutic proteins: Clinical implications and future prospects. Clin Ther 24(11):1720-1740.
    • (2002) Clin Ther , vol.24 , Issue.11 , pp. 1720-1740
    • Schellekens, H.1
  • 17
    • 0034545719 scopus 로고    scopus 로고
    • Quantification and significance of protein oxidation in biological samples
    • Shacter E. 2000. Quantification and significance of protein oxidation in biological samples. Drug Metab Rev 32(3-4):307-326.
    • (2000) Drug Metab Rev , vol.32 , Issue.3-4 , pp. 307-326
    • Shacter, E.1
  • 19
    • 0346100345 scopus 로고    scopus 로고
    • Free radical-mediated oxidation of free amino acids and amino acid residues in proteins
    • Stadtman ER, Levine RL. 2003. Free radical-mediated oxidation of free amino acids and amino acid residues in proteins. Amino Acids 25(3-4):207-218.
    • (2003) Amino Acids , vol.25 , Issue.3-4 , pp. 207-218
    • Stadtman, E.R.1    Levine, R.L.2
  • 20
    • 34249715261 scopus 로고    scopus 로고
    • Oxidation of methionine residues in recombinant human interleukin-1 receptor antagonist: Implications of conformational stability on protein oxidation kinetics
    • Thirumangalathu R, Krishnan S, Bondarenko P, Speed-Ricci M, Randolph TW, Carpenter JF, Brems DN. 2007. Oxidation of methionine residues in recombinant human interleukin-1 receptor antagonist: Implications of conformational stability on protein oxidation kinetics. Biochemistry 46(21):6213-6224.
    • (2007) Biochemistry , vol.46 , Issue.21 , pp. 6213-6224
    • Thirumangalathu, R.1    Krishnan, S.2    Bondarenko, P.3    Speed-Ricci, M.4    Randolph, T.W.5    Carpenter, J.F.6    Brems, D.N.7
  • 21
    • 58149216346 scopus 로고    scopus 로고
    • IgG particle formation during filling pump operation: A case study of heterogeneous nucleation on stainless steel nanoparticles
    • Tyagi AK, Randolph TW, Dong A, Maloney KM, Hitscherich C, Carpenter JF. 2009. IgG particle formation during filling pump operation: A case study of heterogeneous nucleation on stainless steel nanoparticles. J Pharm Sci 98(1):94-104.
    • (2009) J Pharm Sci , vol.98 , Issue.1 , pp. 94-104
    • Tyagi, A.K.1    Randolph, T.W.2    Dong, A.3    Maloney, K.M.4    Hitscherich, C.5    Carpenter, J.F.6
  • 22
    • 33846140780 scopus 로고    scopus 로고
    • Antibody structure, instability, and formulation
    • Wang W, Singh S, Zeng DL, King K, Nema S. 2007. Antibody structure, instability, and formulation. J Pharm Sci 96(1):1-26.
    • (2007) J Pharm Sci , vol.96 , Issue.1 , pp. 1-26
    • Wang, W.1    Singh, S.2    Zeng, D.L.3    King, K.4    Nema, S.5
  • 23
    • 67449132077 scopus 로고    scopus 로고
    • Principles, approaches, and challenges for predicting protein aggregation rates and shelf life
    • Weiss WF, Young TM, Roberts CJ. 2009. Principles, approaches, and challenges for predicting protein aggregation rates and shelf life. J Pharm Sci 98(4):1246-1277.
    • (2009) J Pharm Sci , vol.98 , Issue.4 , pp. 1246-1277
    • Weiss, W.F.1    Young, T.M.2    Roberts, C.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.