메뉴 건너뛰기




Volumn 99, Issue 7, 2010, Pages 2962-2974

Buffer-dependent fragmentation of a humanized full-length monoclonal antibody

Author keywords

Biotechnology; Chemical stability; Formulation; Protein folding refolding; Protein formulation; Proteins

Indexed keywords

BUFFER; HISTIDINE; METAL ION; MONOCLONAL ANTIBODY; TRYPTOPHAN;

EID: 77953317481     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.22056     Document Type: Article
Times cited : (33)

References (45)
  • 1
    • 3843058933 scopus 로고    scopus 로고
    • Commercial manufacturing scale formulation and analytical characterization of therapeutic recombinant antibodies
    • Harris RJ, Shire SJ, Winter C. 2004. Commercial manufacturing scale formulation and analytical characterization of therapeutic recombinant antibodies. Drug Dev Res 61:137-154.
    • (2004) Drug Dev Res , vol.61 , pp. 137-154
    • Harris, R.J.1    Shire, S.J.2    Winter, C.3
  • 2
    • 33747488943 scopus 로고    scopus 로고
    • Formulation and delivery issues for monoclonal antibody therapeutics
    • Daugherty AL, Mrsny RJ. 2006. Formulation and delivery issues for monoclonal antibody therapeutics. Adv Drug Deliv Rev 58:686-706.
    • (2006) Adv Drug Deliv Rev , vol.58 , pp. 686-706
    • Daugherty, A.L.1    Mrsny, R.J.2
  • 4
    • 34848863988 scopus 로고    scopus 로고
    • Characterization of lower molecular weight artifact bands of recombinant monoclonal IgG1 antibodies on non-reducing SDS-PAGE
    • Liu H, Gaza-Bulesco G, Chumase C, Newby-Kew A. 2007. Characterization of lower molecular weight artifact bands of recombinant monoclonal IgG1 antibodies on non-reducing SDS-PAGE. Biotechnol Lett 29:1611-1622.
    • (2007) Biotechnol Lett , vol.29 , pp. 1611-1622
    • Liu, H.1    Gaza-Bulesco, G.2    Chumase, C.3    Newby-Kew, A.4
  • 5
    • 14744289246 scopus 로고    scopus 로고
    • Non-enzymatic hinge region fragmentation of antibodies in solution
    • Cordoba AJ, Shyong B, Breen D, Harris AJ. 2005. Non-enzymatic hinge region fragmentation of antibodies in solution. J Chromatogr B 818:115-121.
    • (2005) J Chromatogr B , vol.818 , pp. 115-121
    • Cordoba, A.J.1    Shyong, B.2    Breen, D.3    Harris, A.J.4
  • 6
    • 46749112184 scopus 로고    scopus 로고
    • Fragmentation of a recombinant monoclonal antibody at various pH
    • Gaza-Bulesco G, Liu H. 2008. Fragmentation of a recombinant monoclonal antibody at various pH. Pharm Res 25:1881-1890.
    • (2008) Pharm Res , vol.25 , pp. 1881-1890
    • Gaza-Bulesco, G.1    Liu, H.2
  • 7
    • 0026463719 scopus 로고
    • Identification of sites of degradation in a therapeutic monoclonal antibody by peptide mapping
    • Kroon DJ, Baldwin-Ferro A, Lalan P. 1992. Identification of sites of degradation in a therapeutic monoclonal antibody by peptide mapping. Pharm Res 9:1386-1393.
    • (1992) Pharm Res , vol.9 , pp. 1386-1393
    • Kroon, D.J.1    Baldwin-Ferro, A.2    Lalan, P.3
  • 8
    • 0028300715 scopus 로고
    • Chemical and physical stability of chimeric L6, a mouse-human monoclonal antibody
    • Paborji M, Pochopin NL, Coppola WP, Bogardus JB. 1994. Chemical and physical stability of chimeric L6, a mouse-human monoclonal antibody. Pharm Res 11:764-771.
    • (1994) Pharm Res , vol.11 , pp. 764-771
    • Paborji, M.1    Pochopin, N.L.2    Coppola, W.P.3    Bogardus, J.B.4
  • 9
    • 0028787777 scopus 로고
    • Monitoring of IgG antibody thermal stability by micellar electrokinetic capillary chromatography and matrix-assisted laser desorption/ionization mass spectrometry
    • Alexander AJ, Hughes DE. 1995. Monitoring of IgG antibody thermal stability by micellar electrokinetic capillary chromatography and matrix-assisted laser desorption/ionization mass spectrometry. Anal Chem 67:3626-3632.
    • (1995) Anal Chem , vol.67 , pp. 3626-3632
    • Alexander, A.J.1    Hughes, D.E.2
  • 10
    • 33744466598 scopus 로고    scopus 로고
    • Characterization of the stability of a fully human monoclonal IgG after prolonged incubation at elevated temperature
    • Liu H, Gaza-Bulesco G, Sun J. 2006. Characterization of the stability of a fully human monoclonal IgG after prolonged incubation at elevated temperature. J Chromatogr B 837:35-43.
    • (2006) J Chromatogr B , vol.837 , pp. 35-43
    • Liu, H.1    Gaza-Bulesco, G.2    Sun, J.3
  • 11
    • 30744439811 scopus 로고    scopus 로고
    • Influence of pH buffer species, and storage temperature on physicochemical stability of a humanized monoclonal antibody LA298
    • Zheng JY, Janis LJ. 2006. Influence of pH, buffer species, and storage temperature on physicochemical stability of a humanized monoclonal antibody LA298. Int J Pharm 308:46-51.
    • (2006) Int J Pharm , vol.308 , pp. 46-51
    • Zheng, J.Y.1    Janis, L.J.2
  • 12
    • 0032924058 scopus 로고    scopus 로고
    • A mechanistic analysis of the increase in the thermal stability of proteins in aqueous carboxylic acid salt solutions
    • Kaushik JK, Bhat R. 1999. A mechanistic analysis of the increase in the thermal stability of proteins in aqueous carboxylic acid salt solutions. Protein Sci 8:222-233.
    • (1999) Protein Sci , vol.8 , pp. 222-233
    • Kaushik, J.K.1    Bhat, R.2
  • 14
    • 0346846691 scopus 로고    scopus 로고
    • Influence of histidine on the stability and physical properties of a fully human antibody in aqueous and solid forms
    • Chen B, Bautista R, Yu K, Zapata GA, Mulkerrin MG, Chamow SM. 2003. Influence of histidine on the stability and physical properties of a fully human antibody in aqueous and solid forms. Pharm Res 20:1952-1960.
    • (2003) Pharm Res , vol.20 , pp. 1952-1960
    • Chen, B.1    Bautista, R.2    Yu, K.3    Zapata, G.A.4    Mulkerrin, M.G.5    Chamow, S.M.6
  • 15
    • 33344472283 scopus 로고    scopus 로고
    • Calorimetric investigation of protein/amino acid interactions in the solid state
    • DOI 10.1016/j.ijpharm.2005.12.009, PII S037851730500815X
    • Tian F, Sane S, Rytting JH. 2006. Calorimetric investigation of protein/amino acid interactions in the solid state. Int J Pharm 310:175-186. (Pubitemid 43287982)
    • (2006) International Journal of Pharmaceutics , vol.310 , Issue.1-2 , pp. 175-186
    • Tian, F.1    Sane, S.2    Rytting, J.H.3
  • 17
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace CN. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131:266-280.
    • (1986) Methods Enzymol , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 18
    • 0033551522 scopus 로고    scopus 로고
    • Observation of multistate kinetics during the slow folding and unfolding of barstar
    • Bhuyan AK, Udgaonkar JB. 1999. Observation of multistate kinetics during the slow folding and unfolding of barstar. Biochemistry 38:9158-9168. (Pubitemid 129515250)
    • (1999) Biochemistry , vol.38 , Issue.28 , pp. 9158-9168
    • Bhuyan, A.K.1    Udgaonkar, J.B.2
  • 19
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence - Quenching of tryptophyl fluorescence of model compounds and of lysozyme by iodide ion
    • Lehrer SS. 1971. Solute perturbation of protein fluorescence - Quenching of tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 10:3254-3263.
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.S.1
  • 20
    • 0002388667 scopus 로고
    • On the quenching time of fluorescence
    • Stern OAMV. 1919. On the quenching time of fluorescence. Z Phys 20:183-199.
    • (1919) Z Phys , vol.20 , pp. 183-199
    • Stern, O.A.M.V.1
  • 21
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • DOI 10.1023/A:1025771421906
    • Chi EY, Krishnan S, Randolph TW, Carpenter JF. 2003. Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation. Pharm Res 20:1325-1336. (Pubitemid 37164039)
    • (2003) Pharmaceutical Research , vol.20 , Issue.9 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 22
    • 0242515822 scopus 로고    scopus 로고
    • Roles of conformational and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor
    • Chi EY, Krishnan S, Kendrick BS, Chang BS, Carpenter JF, Randolph TW. 2003. Roles of conformational and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor. Protein Sci 12:1903-1913.
    • (2003) Protein Sci , vol.12 , pp. 1903-1913
    • Chi, E.Y.1    Krishnan, S.2    Kendrick, B.S.3    Chang, B.S.4    Carpenter, J.F.5    Randolph, T.W.6
  • 23
    • 0034076282 scopus 로고    scopus 로고
    • The thermal stability of immunoglobulin: Unfolding and aggregation of a multi-domain protein
    • Vermeer AWP, Norde W. 2000. The thermal stability of immunoglobulin: Unfolding and aggregation of a multi-domain protein. Biophys J 78:394-404.
    • (2000) Biophys J , vol.78 , pp. 394-404
    • Vermeer, A.W.P.1    Norde, W.2
  • 24
    • 0033649068 scopus 로고    scopus 로고
    • Linear extrapolation method of analyzing solvent denaturation curves
    • Pace CN, Shaw KL. 2000. Linear extrapolation method of analyzing solvent denaturation curves. Proteins 4:1-7.
    • (2000) Proteins , vol.4 , pp. 1-7
    • Pace, C.N.1    Shaw, K.L.2
  • 29
    • 0036360325 scopus 로고    scopus 로고
    • Effects of conformation on the chemical stability of pharmaceutically relevant polypeptides
    • Meyer JD, Ho B, Manning MC. 2002. Effects of conformation on the chemical stability of pharmaceutically relevant polypeptides. Pharm Biotechnol 13:85-107.
    • (2002) Pharm Biotechnol , vol.13 , pp. 85-107
    • Meyer, J.D.1    Ho, B.2    Manning, M.C.3
  • 31
    • 33845960288 scopus 로고    scopus 로고
    • Comparative oxidation studies of methionine residues reflect a structural effect on chemical kinetics in rhG-CSF
    • Pan B, Abel J, Ricci MS, Brems DN, Wang DIC, Trout BL. 2006. Comparative oxidation studies of methionine residues reflect a structural effect on chemical kinetics in rhG-CSF. Biochemistry 45:15430-15443.
    • (2006) Biochemistry , vol.45 , pp. 15430-15443
    • Pan, B.1    Abel, J.2    Ricci, M.S.3    Brems, D.N.4    Wang, D.I.C.5    Trout, B.L.6
  • 32
    • 0030176302 scopus 로고    scopus 로고
    • The effect of pH, hydrogen peroxide and temperature on the stability of human monoclonal antibody
    • DOI 10.1016/S0731-7085(96)01721-9
    • Usami A, Ohtsu A, Takahama S, Fujii T. 1996. Effect of pH, hydrogen peroxide and temperature on the stability of human monoclonal antibody. J Pharm Biomed Anal 14:1133-1140. (Pubitemid 26235167)
    • (1996) Journal of Pharmaceutical and Biomedical Analysis , vol.14 , Issue.8-10 , pp. 1133-1140
    • Usami, A.1    Ohtsu, A.2    Takahama, S.3    Fujii, T.4
  • 33
    • 77953297675 scopus 로고
    • The hydrolysis of proteins and peptones at high temperatures and the catalytic effect of metal ions on the rate of hydrolysis
    • Lieben F. 1943. The hydrolysis of proteins and peptones at high temperatures and the catalytic effect of metal ions on the rate of hydrolysis. J Biol Chem 151:117-121.
    • (1943) J Biol Chem , vol.151 , pp. 117-121
    • Lieben, F.1
  • 35
    • 33744718161 scopus 로고    scopus 로고
    • Major advances in the hydrolysis of peptides and proteins by metal ions and complexes
    • DOI 10.2174/138527206777435535
    • Grant KB, Kassai M. 2006. Major advances in the hydrolysis of peptides and proteins by metal ions and complexes. Curr Org Chem 10:1035-1049. (Pubitemid 43821682)
    • (2006) Current Organic Chemistry , vol.10 , Issue.9 , pp. 1035-1049
    • Grant, K.B.1    Kassai, M.2
  • 36
    • 0032558362 scopus 로고    scopus 로고
    • Mutual stabilization of V(L) and V(H) in single-chain antibody fragments, investigated with mutants engineered for stability
    • DOI 10.1021/bi980712q
    • Wörn A, Plückthun A. 1998. Mutual stabilization of VL and VH in single-chain antibody fragments, investigated with mutants engineered for stability. Biochemistry 37:13120-13127. (Pubitemid 28449555)
    • (1998) Biochemistry , vol.37 , Issue.38 , pp. 13120-13127
    • Worn, A.1    Pluckthun, A.2
  • 37
    • 0033042555 scopus 로고    scopus 로고
    • Stability and folding of domain proteins
    • Jaenicke R. 1999. Stability and folding of domain proteins. Prog Biophys Mol Biol 71:155-241.
    • (1999) Prog Biophys Mol Biol , vol.71 , pp. 155-241
    • Jaenicke, R.1
  • 38
    • 0345044918 scopus 로고    scopus 로고
    • Domain interactions in antibody Fv and scFv fragments: Effects on kinetics and equilibria
    • Jäger M, Plückthun A. 1999. Domain interactions in antibody Fv and scFv fragments: Effects on kinetics and equilibria. FEBS Lett 462:307-312.
    • (1999) FEBS Lett , vol.462 , pp. 307-312
    • Jäger, M.1    Plückthun, A.2
  • 39
    • 0037031314 scopus 로고    scopus 로고
    • Four-state equilibrium unfolding of an scFv antibody fragment
    • DOI 10.1021/bi025742e
    • Pedroso I, Irún MP, Machicado C, Sancho J. 2002. Four-state equilibriumunfolding of scFv antibody fragment. Biochemistry 41:9873-9884. (Pubitemid 34839735)
    • (2002) Biochemistry , vol.41 , Issue.31 , pp. 9873-9884
    • Pedroso, I.1    Irun, M.P.2    Machicado, C.3    Sancho, J.4
  • 40
    • 33847416982 scopus 로고    scopus 로고
    • A broad range of Fab stabilities within a host of therapeutic IgGs
    • DOI 10.1016/j.bbrc.2007.02.042, PII S0006291X07002975
    • Garber E, Demarest SJ. 2007. A broad range of Fab stabilities within a host of therapeutic IgGs. Biochem Biophys Res Commun 355:751-757. (Pubitemid 46343718)
    • (2007) Biochemical and Biophysical Research Communications , vol.355 , Issue.3 , pp. 751-757
    • Garber, E.1    Demarest, S.J.2
  • 41
    • 0024973030 scopus 로고
    • A simple model for proteins with interacting domains. Applications to scanning calorimetry data
    • Brandts JF, Hu CQ, Lin L. 1989. A simple model for proteins with interacting domains. Applications to scanning calorimetry data. Biochemistry 28:8588-8596.
    • (1989) Biochemistry , vol.28 , pp. 8588-8596
    • Brandts, J.F.1    Hu, C.Q.2    Lin, L.3
  • 42
    • 33744912751 scopus 로고    scopus 로고
    • Cooperative unfolding of Escherichia coli ribosome recycling factor originating from its domain-domain interaction and its implication for function
    • DOI 10.1016/j.abb.2006.03.029, PII S0003986106001342
    • Zhang L, Guo P, Zhang H, Jing G. 2006. Cooperative unfolding of Escherichia coli ribosome recycling factor originating from its domain - domain interaction and its implication for function. Arch Biochem Biophys 450:191-202. (Pubitemid 43849627)
    • (2006) Archives of Biochemistry and Biophysics , vol.450 , Issue.2 , pp. 191-202
    • Zhang, L.1    Guo, P.2    Zhang, H.3    Jing, G.4
  • 43
    • 50649104170 scopus 로고    scopus 로고
    • Transition metal ion binding studies of carnosine and histidine: Biologically relevant antioxidants
    • Velez S, Nair NG, Reddy VP. 2008. Transition metal ion binding studies of carnosine and histidine: Biologically relevant antioxidants. Colloids Surf B 66:291-294.
    • (2008) Colloids Surf B , vol.66 , pp. 291-294
    • Velez, S.1    Nair, N.G.2    Reddy, V.P.3
  • 44
    • 0000438565 scopus 로고
    • Washington, DC: American Chemical Society
    • Sigel H. 1989. Metal-DNA chemistry. Washington, DC: American Chemical Society.
    • (1989) Metal-DNA Chemistry
    • Sigel, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.