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Volumn 96, Issue 1, 2007, Pages 1-26

Antibody structure, instability, and formulation

Author keywords

Biotechnology; Freeze drying lyophilization; Protein aggregation; Protein formulation; Stabilization

Indexed keywords

ABCIXIMAB; ADALIMUMAB; ALEMTUZUMAB; ARCITUMOMAB TC 99M; BASILIXIMAB; BEVACIZUMAB; CAPROMAB PENDETIDE IN 111; CETUXIMAB; DACLIZUMAB; EFALIZUMAB; GEMTUZUMAB OZOGAMICIN; IBRITUMOMAB TIUXETAN; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G2; IMMUNOGLOBULIN G2A; INFLIXIMAB; INTERLEUKIN 8 ANTIBODY; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY B.72.3; NATALIZUMAB; NOFETUMOMAB; OKT 3; OMALIZUMAB; ONCOSCINT; ORTHOCLONE OKT; PALIVIZUMAB; PERTUZUMAB; RANIBIZUMAB; RITUXIMAB; TOSITUMOMAB I 131; TRASTUZUMAB; UNCLASSIFIED DRUG; UNINDEXED DRUG; VERLUMA;

EID: 33846140780     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.20727     Document Type: Short Survey
Times cited : (793)

References (115)
  • 1
    • 0034854492 scopus 로고    scopus 로고
    • Effect of moisture on the stability of a lyophilized humanized monoclonal antibody formulation
    • Breen ED, Curley JG, Overcashier DE, Hsu CC, Shire SJ. 2001. Effect of moisture on the stability of a lyophilized humanized monoclonal antibody formulation. Pharm Res 18:1345-1353.
    • (2001) Pharm Res , vol.18 , pp. 1345-1353
    • Breen, E.D.1    Curley, J.G.2    Overcashier, D.E.3    Hsu, C.C.4    Shire, S.J.5
  • 2
    • 2942722679 scopus 로고    scopus 로고
    • Antibodies and genetically engineered related molecules: Production and purification
    • Roque ACA, Lowe CR, Taipa MA. 2004. Antibodies and genetically engineered related molecules: Production and purification. Biotechnol Prog 20:639-654.
    • (2004) Biotechnol Prog , vol.20 , pp. 639-654
    • Roque, A.C.A.1    Lowe, C.R.2    Taipa, M.A.3
  • 3
    • 14844285410 scopus 로고    scopus 로고
    • The therapeutic antibodies market to 2008
    • Pavlou AK, Belsey MJ. 2005. The therapeutic antibodies market to 2008. Eur J Pharm Biopharm 59:389-396.
    • (2005) Eur J Pharm Biopharm , vol.59 , pp. 389-396
    • Pavlou, A.K.1    Belsey, M.J.2
  • 5
    • 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
  • 7
    • 0035988060 scopus 로고    scopus 로고
    • Free sulfhydryl in recombinant monoclonal antibodies
    • Zhang W, Czupryn MJ. 2002. Free sulfhydryl in recombinant monoclonal antibodies. Biotechnol Prog 18:509-513.
    • (2002) Biotechnol Prog , vol.18 , pp. 509-513
    • Zhang, W.1    Czupryn, M.J.2
  • 9
    • 0026572809 scopus 로고
    • The disulfide bonds in antibody variable domains: Effects on stability, folding in vitro, and functional expression in Escherichia coli
    • Glockshuber R, Schmidt T, Pluckthun A. 1992. The disulfide bonds in antibody variable domains: Effects on stability, folding in vitro, and functional expression in Escherichia coli. Biochemistry 31:1270-1279.
    • (1992) Biochemistry , vol.31 , pp. 1270-1279
    • Glockshuber, R.1    Schmidt, T.2    Pluckthun, A.3
  • 10
    • 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
  • 11
    • 0031033895 scopus 로고    scopus 로고
    • Effect of glycosylation on antibody function: Implications for genetic engineering
    • Wright A, Morrison SL. 1997. Effect of glycosylation on antibody function: Implications for genetic engineering. Trends Biotechnol 15:26-32.
    • (1997) Trends Biotechnol , vol.15 , pp. 26-32
    • Wright, A.1    Morrison, S.L.2
  • 12
    • 0024438061 scopus 로고
    • Studies of aglycosylated chimeric mouse-human IgG. Role of carbohydrate in the structure and effector functions mediated by the human IgG constant region
    • Tao MH, Morrison SL. 1989. Studies of aglycosylated chimeric mouse-human IgG. Role of carbohydrate in the structure and effector functions mediated by the human IgG constant region. J Immunol 143:2595-2601.
    • (1989) J Immunol , vol.143 , pp. 2595-2601
    • Tao, M.H.1    Morrison, S.L.2
  • 13
    • 0039725069 scopus 로고    scopus 로고
    • Variable domain-linked oligosaccharides of a human monoclonal IgG: Structure and influence on antigen binding
    • Leibiger H, Wustner D, Stigler RD, Marx U. 1999. Variable domain-linked oligosaccharides of a human monoclonal IgG: Structure and influence on antigen binding. Biochem J 338:529-538.
    • (1999) Biochem J , vol.338 , pp. 529-538
    • Leibiger, H.1    Wustner, D.2    Stigler, R.D.3    Marx, U.4
  • 15
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • Shinkawa T, Nakamura K, Yamane N, Shoji-Hosaka E, Kanda Y, Sakurada M, Uchida K, Anazawa H, Satoh M, Yamasaki M, Hanai N, Shitara K. 2003. The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J Biol Chem 278:3466-3473.
    • (2003) J Biol Chem , vol.278 , pp. 3466-3473
    • Shinkawa, T.1    Nakamura, K.2    Yamane, N.3    Shoji-Hosaka, E.4    Kanda, Y.5    Sakurada, M.6    Uchida, K.7    Anazawa, H.8    Satoh, M.9    Yamasaki, M.10    Hanai, N.11    Shitara, K.12
  • 16
    • 0030582305 scopus 로고    scopus 로고
    • Capillary isoelectric focusing and sodium dodecyl sulfatecapillary gel electrophoresis of recombinant humanized monoclonal antibody HER2
    • Hunt G, Moorhouse KG, Chen AB. 1996. Capillary isoelectric focusing and sodium dodecyl sulfatecapillary gel electrophoresis of recombinant humanized monoclonal antibody HER2. J Chromatogr A 744:295-301.
    • (1996) J Chromatogr A , vol.744 , pp. 295-301
    • Hunt, G.1    Moorhouse, K.G.2    Chen, A.B.3
  • 18
    • 23844454990 scopus 로고    scopus 로고
    • Structural characterization of a recombinant monoclonal antibody by electrospray time-of-flight mass spectrometry
    • Wang L, Amphlett G, Lambert JM, Blattler W, Zhang W. 2005. Structural characterization of a recombinant monoclonal antibody by electrospray time-of-flight mass spectrometry. Pharm Res 22:1338-1349.
    • (2005) Pharm Res , vol.22 , pp. 1338-1349
    • Wang, L.1    Amphlett, G.2    Lambert, J.M.3    Blattler, W.4    Zhang, W.5
  • 19
  • 20
    • 0036760452 scopus 로고    scopus 로고
    • Crystal structures of human antibodies: A detailed and unfinished tapestry of immunoglobulin gene products
    • Ramsland PA, Farrugia W. 2002. Crystal structures of human antibodies: A detailed and unfinished tapestry of immunoglobulin gene products. J Mol Recognit 15:248-259.
    • (2002) J Mol Recognit , vol.15 , pp. 248-259
    • Ramsland, P.A.1    Farrugia, W.2
  • 21
    • 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, Chamow SM, et al. 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    Chamow, S.M.5
  • 22
    • 2142643646 scopus 로고    scopus 로고
    • Solution structure determination of monomeric human IgA2 by X-ray and neutron scattering, analytical ultracentrifugation and constrained modelling: A comparison with monomeric human IgAl
    • Furtado PB, Whitty PW, Robertson A, Eaton JT, Almogren A, Kerr MA, Woof JM, Perkins SJ. 2004. Solution structure determination of monomeric human IgA2 by X-ray and neutron scattering, analytical ultracentrifugation and constrained modelling: A comparison with monomeric human IgAl. J Mol Biol 338:921-941.
    • (2004) J Mol Biol , vol.338 , pp. 921-941
    • Furtado, P.B.1    Whitty, P.W.2    Robertson, A.3    Eaton, J.T.4    Almogren, A.5    Kerr, M.A.6    Woof, J.M.7    Perkins, S.J.8
  • 23
    • 0024694268 scopus 로고
    • Practical considerations in the production, purification, and formulation of monoclonal antibodies for immunoscintigraphy and immunotherapy
    • Bogard WC, Jr., Dean RT, Deo Y, Fuchs R, Mattis JA, McLean AA, Berger HJ. 1989. Practical considerations in the production, purification, and formulation of monoclonal antibodies for immunoscintigraphy and immunotherapy. Semin Nucl Med 19:202-220.
    • (1989) Semin Nucl Med , vol.19 , pp. 202-220
    • Bogard Jr., W.C.1    Dean, R.T.2    Deo, Y.3    Fuchs, R.4    Mattis, J.A.5    McLean, A.A.6    Berger, H.J.7
  • 24
    • 0032558362 scopus 로고    scopus 로고
    • Mutual stabilization of VL and VH in single-chain antibody fragments, investigated with mutants engineered for stability
    • Worn A, Pluckthun A. 1998. Mutual stabilization of VL and VH in single-chain antibody fragments, investigated with mutants engineered for stability. Biochemistry 37:13120-13127.
    • (1998) Biochemistry , vol.37 , pp. 13120-13127
    • Worn, A.1    Pluckthun, A.2
  • 25
    • 0032581013 scopus 로고    scopus 로고
    • Contribution of domain interface residues to the stability of antibody CH3 domain homodimers
    • Dall'Acqua W, Simon AL, Mulkerrin MG, Carter P. 1998. Contribution of domain interface residues to the stability of antibody CH3 domain homodimers. Biochemistry 37:9266-9273.
    • (1998) Biochemistry , vol.37 , pp. 9266-9273
    • Dall'Acqua, W.1    Simon, A.L.2    Mulkerrin, M.G.3    Carter, P.4
  • 26
    • 2942560478 scopus 로고    scopus 로고
    • Variable region domain exchange in human IgGs promotes antibody complex formation with accompanying structural changes and altered effector functions
    • Chan LA, Phillips ML, Wims LA, Trinh KR, Denham J, Morrison SL. 2004. Variable region domain exchange in human IgGs promotes antibody complex formation with accompanying structural changes and altered effector functions. Mol Immunol 41:527-538.
    • (2004) Mol Immunol , vol.41 , pp. 527-538
    • Chan, L.A.1    Phillips, M.L.2    Wims, L.A.3    Trinh, K.R.4    Denham, J.5    Morrison, S.L.6
  • 28
    • 0032568959 scopus 로고    scopus 로고
    • Automated classification of antibody complementarity determining region 3 of the heavy chain (h3) loops into canonical forms and its application to protein structure prediction
    • Oliva B, Bates PA, Querol E, Aviles FX, Sternberg MJE. 1998. Automated classification of antibody complementarity determining region 3 of the heavy chain (h3) loops into canonical forms and its application to protein structure prediction. J Mol Biol 279:1193-1210.
    • (1998) J Mol Biol , vol.279 , pp. 1193-1210
    • Oliva, B.1    Bates, P.A.2    Querol, E.3    Aviles, F.X.4    Sternberg, M.J.E.5
  • 31
    • 0030604686 scopus 로고    scopus 로고
    • X-ray structure of the uncomplexed antitumor antibody br96 and comparison with its antigen-bound form
    • Sheriff S, Chang CYY, Jeffrey PD, Bajorath J. 1996. X-ray structure of the uncomplexed antitumor antibody br96 and comparison with its antigen-bound form. J Mol Biol 259:938-946.
    • (1996) J Mol Biol , vol.259 , pp. 938-946
    • Sheriff, S.1    Chang, C.Y.Y.2    Jeffrey, P.D.3    Bajorath, J.4
  • 32
    • 0036760872 scopus 로고    scopus 로고
    • Reductionism and the search for structure-function relationships in antibody molecules
    • Van Regenmortel MHV. 2002. Reductionism and the search for structure-function relationships in antibody molecules. J Mol Recognit 15:240-247.
    • (2002) J Mol Recognit , vol.15 , pp. 240-247
    • Van Regenmortel, M.H.V.1
  • 33
    • 8644234910 scopus 로고    scopus 로고
    • Antibody pharmacokinetics and pharmacodynamics
    • Lobo ED, Hansen RJ, Balthasar JP. 2004. Antibody pharmacokinetics and pharmacodynamics. J Pharm Sci 93:2645-2668.
    • (2004) J Pharm Sci , vol.93 , pp. 2645-2668
    • Lobo, E.D.1    Hansen, R.J.2    Balthasar, J.P.3
  • 34
    • 0031568069 scopus 로고    scopus 로고
    • The hinge as a spacer contributes to covalent assembly and is required for function of IgG
    • Coloma MJ, Trinh KR, Wims LA, Morrison SL. 1997. The hinge as a spacer contributes to covalent assembly and is required for function of IgG. J Immunol 158:733-740.
    • (1997) J Immunol , vol.158 , pp. 733-740
    • Coloma, M.J.1    Trinh, K.R.2    Wims, L.A.3    Morrison, S.L.4
  • 35
    • 0142087554 scopus 로고    scopus 로고
    • Antibodies as therapeutic agents: Vive la renaissance!
    • Stockwin LH, Holmes S. 2003. Antibodies as therapeutic agents: Vive la renaissance! Expert Opin Biol Ther 3:1133-1152.
    • (2003) Expert Opin Biol Ther , vol.3 , pp. 1133-1152
    • Stockwin, L.H.1    Holmes, S.2
  • 36
    • 0030022071 scopus 로고    scopus 로고
    • Isomerization of an aspartic acid residue in the complementarity-determining regions of a recombinant antibody to human IgE: Identification and effect on binding affinity
    • Cacia J, Keck R, Presta LG, Frenz J. 1996. Isomerization of an aspartic acid residue in the complementarity-determining regions of a recombinant antibody to human IgE: Identification and effect on binding affinity. Biochemistry 35:1897-1903.
    • (1996) Biochemistry , vol.35 , pp. 1897-1903
    • Cacia, J.1    Keck, R.2    Presta, L.G.3    Frenz, J.4
  • 39
    • 4143137525 scopus 로고    scopus 로고
    • Effect of linker sequences between the antibody variable domains on the formation, stability and biological activity of a bispecific tandem diabody
    • Le Gall F, Reusch U, Little M, Kipriyanov SM. 2004. Effect of linker sequences between the antibody variable domains on the formation, stability and biological activity of a bispecific tandem diabody. Protein Eng Des Sel 17:85-93.
    • (2004) Protein Eng Des Sel , vol.17 , pp. 85-93
    • Le Gall, F.1    Reusch, U.2    Little, M.3    Kipriyanov, S.M.4
  • 40
    • 33846158843 scopus 로고    scopus 로고
    • Protein formulation of an IGG1 antibody with atypical glycosylation: A study on the stability of its glycoforms
    • Chu GC, Coulibaly SB, Raibekas A, Deechongkit S. 2005. Protein formulation of an IGG1 antibody with atypical glycosylation: A study on the stability of its glycoforms. Abstr Pap Am Chem Soc 229:U210-U211.
    • (2005) Abstr Pap Am Chem Soc , vol.229
    • Chu, G.C.1    Coulibaly, S.B.2    Raibekas, A.3    Deechongkit, S.4
  • 41
    • 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
  • 42
    • 0032940238 scopus 로고    scopus 로고
    • Conformation, pH-induced conformational changes, and thermal unfolding of anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab and Fc fragments
    • Welfle K, Misselwitz R, Hausdorf G, Hohne W, Welfle H. 1999. Conformation, pH-induced conformational changes, and thermal unfolding of anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab and Fc fragments. Biochim Biophys Acta 1431:120-131.
    • (1999) Biochim Biophys Acta , vol.1431 , pp. 120-131
    • Welfle, K.1    Misselwitz, R.2    Hausdorf, G.3    Hohne, W.4    Welfle, H.5
  • 43
    • 13244259221 scopus 로고    scopus 로고
    • Effects of pulsed electric fields and heat treatment on stability and secondary structure of bovine immunoglobulin G
    • Li SQ, Bomser JA, Zhang QH. 2005. Effects of pulsed electric fields and heat treatment on stability and secondary structure of bovine immunoglobulin G. J Agric Food Chem 53:663-670.
    • (2005) J Agric Food Chem , vol.53 , pp. 663-670
    • Li, S.Q.1    Bomser, J.A.2    Zhang, Q.H.3
  • 44
    • 0032782071 scopus 로고    scopus 로고
    • Instability, stabilization, and formulation of liquid protein pharmaceuticals
    • Wang W. 1999. Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int J Pharm 185:129-188.
    • (1999) Int J Pharm , vol.185 , pp. 129-188
    • Wang, W.1
  • 45
    • 0032552164 scopus 로고    scopus 로고
    • Stability of a single-chain Fv antibody fragment when exposed to a high shear environment combined with air-liquid interfaces
    • Harrison JS, Gill A, Hoare M. 1998. Stability of a single-chain Fv antibody fragment when exposed to a high shear environment combined with air-liquid interfaces. Biotechnol Bioeng 59:517-519.
    • (1998) Biotechnol Bioeng , vol.59 , pp. 517-519
    • Harrison, J.S.1    Gill, A.2    Hoare, M.3
  • 47
    • 2642550862 scopus 로고    scopus 로고
    • Challenges in the development of high protein concentration formulations
    • Shire SJ, Shahrokh Z, Liu J. 2004. Challenges in the development of high protein concentration formulations. J Pharm Sci 93:1390-1402.
    • (2004) J Pharm Sci , vol.93 , pp. 1390-1402
    • Shire, S.J.1    Shahrokh, Z.2    Liu, J.3
  • 48
    • 0030856842 scopus 로고    scopus 로고
    • Protein aggregates seem to play a key role among the parameters influencing the antigenicity of interferon alpha (IFN-alpha) in normal and transgenic mice
    • Braun A, Kwee L, Labow MA, Alsenz J. 1997. Protein aggregates seem to play a key role among the parameters influencing the antigenicity of interferon alpha (IFN-alpha) in normal and transgenic mice. Pharm Res 14:1472-1478.
    • (1997) Pharm Res , vol.14 , pp. 1472-1478
    • Braun, A.1    Kwee, L.2    Labow, M.A.3    Alsenz, J.4
  • 50
    • 0030069525 scopus 로고    scopus 로고
    • Adverse effects of intravenous immunoglobuin therapy
    • Ryan ME, Webster ML, Statler JD. 1996. Adverse effects of intravenous immunoglobuin therapy. Clin Pediatr 35:23-31.
    • (1996) Clin Pediatr , vol.35 , pp. 23-31
    • Ryan, M.E.1    Webster, M.L.2    Statler, J.D.3
  • 51
    • 0036468995 scopus 로고    scopus 로고
    • Kinetic studies of protein-protein interactions
    • Schreiber G. 2002. Kinetic studies of protein-protein interactions. Curr Opin Struct Biol 12:41-47.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 41-47
    • Schreiber, G.1
  • 52
    • 3242670796 scopus 로고    scopus 로고
    • Opalescent appearance of an IgG1 antibody at high concentrations and its relationship to noncovalent association
    • Sukumar M, Doyle BL, Combs JL, Pekar AH. 2004. Opalescent appearance of an IgG1 antibody at high concentrations and its relationship to noncovalent association. Pharm Res 21:1087-1093.
    • (2004) Pharm Res , vol.21 , pp. 1087-1093
    • Sukumar, M.1    Doyle, B.L.2    Combs, J.L.3    Pekar, A.H.4
  • 53
    • 0025892154 scopus 로고
    • Use of surface tension measurements in the design of antibody-based product formulations
    • Levine HL, Ransohoff TC, Kawahata RT, McGregor WC. 1991. Use of surface tension measurements in the design of antibody-based product formulations. J Parenter Sci Technol 45:160-165.
    • (1991) J Parenter Sci Technol , vol.45 , pp. 160-165
    • Levine, H.L.1    Ransohoff, T.C.2    Kawahata, R.T.3    McGregor, W.C.4
  • 56
    • 33846125282 scopus 로고    scopus 로고
    • Stabilized monomeric protein compositions. Enzon, Inc.,
    • US Patent US 5656730
    • Lee LS. 1997. Stabilized monomeric protein compositions. Enzon, Inc., US Patent US 5656730.
    • (1997)
    • Lee, L.S.1
  • 58
    • 33846156570 scopus 로고    scopus 로고
    • human monoclonal antibody preparation, Yoshihide Hagiwara
    • Hagiwara H, Yuasa H, Yamamoto Y. 2000. Stabilized human monoclonal antibody preparation, Yoshihide Hagiwara.
    • (2000) Stabilized
    • Hagiwara, H.1    Yuasa, H.2    Yamamoto, Y.3
  • 59
    • 0026546749 scopus 로고
    • Influence of sucrose, dextran, and hydroxypropyl-beta-cyclodextrin as lyoprotectants for a freeze-dried mouse IgG2a monoclonal antibody (MN12)
    • Ressing ME, Jiskoot W, Talsma H, Van Ingen CW, Crommelin DJ, et al. 1992. Influence of sucrose, dextran, and hydroxypropyl-beta-cyclodextrin as lyoprotectants for a freeze-dried mouse IgG2a monoclonal antibody (MN12). Pharm Res 9:266-270.
    • (1992) Pharm Res , vol.9 , pp. 266-270
    • Ressing, M.E.1    Jiskoot, W.2    Talsma, H.3    Van Ingen, C.W.4    Crommelin, D.J.5
  • 60
    • 0026356940 scopus 로고
    • The effects of formulation and moisture on the stability of a freeze-dried monoclonal antibody-vinca conjugate: A test of the WLF glass transition theory
    • discussion 340
    • Roy ML, Pikal MJ, Rickard EC, Maloney AM. 1992. The effects of formulation and moisture on the stability of a freeze-dried monoclonal antibody-vinca conjugate: A test of the WLF glass transition theory. Dev Biol Stand 74:323-339; discussion 340.
    • (1992) Dev Biol Stand , vol.74 , pp. 323-339
    • Roy, M.L.1    Pikal, M.J.2    Rickard, E.C.3    Maloney, A.M.4
  • 61
    • 0030329632 scopus 로고    scopus 로고
    • Formulation development of an antifibrin monoclonal antibody, radiopharmaceutical
    • Kamat MS, Tolman GL, Brown JM. 1996. Formulation development of an antifibrin monoclonal antibody, radiopharmaceutical. Pharm Biotechnol 9:343-364.
    • (1996) Pharm Biotechnol , vol.9 , pp. 343-364
    • Kamat, M.S.1    Tolman, G.L.2    Brown, J.M.3
  • 62
    • 55449104956 scopus 로고    scopus 로고
    • Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations
    • Andya JD, Hsu CC, Shire SJ. 2003. Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations. AAPS PharmSci 5:E10.
    • (2003) AAPS PharmSci , vol.5
    • Andya, J.D.1    Hsu, C.C.2    Shire, S.J.3
  • 63
    • 0025824432 scopus 로고
    • Solution stability of the monoclonal antibody-vinca alkaloid conjugate, KS1/4-DAVLB
    • Riggin A, Clodfelter D, Maloney A, Rickard E, Massey E. 1991. Solution stability of the monoclonal antibody-vinca alkaloid conjugate, KS1/4-DAVLB. Pharm Res 8:1264-1269.
    • (1991) Pharm Res , vol.8 , pp. 1264-1269
    • Riggin, A.1    Clodfelter, D.2    Maloney, A.3    Rickard, E.4    Massey, E.5
  • 64
    • 0030961777 scopus 로고    scopus 로고
    • Effect of glass transition temperature on the stability of lyophilized formulations containing a chimeric therapeutic monoclonal antibody
    • Duddu SP, Dal Monte PR. 1997. Effect of glass transition temperature on the stability of lyophilized formulations containing a chimeric therapeutic monoclonal antibody. Pharm Res 14:591-595.
    • (1997) Pharm Res , vol.14 , pp. 591-595
    • Duddu, S.P.1    Dal Monte, P.R.2
  • 65
    • 0031780284 scopus 로고    scopus 로고
    • Effect of spray drying and subsequent processing conditions on residual moisture content and physical/biochemical stability of protein inhalation powders
    • Maa YF, Nguyen PA, Andya JD, Dasovich N, Hsu CC, et al. 1998. Effect of spray drying and subsequent processing conditions on residual moisture content and physical/biochemical stability of protein inhalation powders. Pharm Res 15:768-775.
    • (1998) Pharm Res , vol.15 , pp. 768-775
    • Maa, Y.F.1    Nguyen, P.A.2    Andya, J.D.3    Dasovich, N.4    Hsu, C.C.5
  • 66
    • 0031914743 scopus 로고    scopus 로고
    • Spray-drying of air-liquid interface sensitive recombinant human growth hormone
    • Maa YF, Nguyen PA, Hsu SW. 1998. Spray-drying of air-liquid interface sensitive recombinant human growth hormone. J Pharm Sci 87:152-159.
    • (1998) J Pharm Sci , vol.87 , pp. 152-159
    • Maa, Y.F.1    Nguyen, P.A.2    Hsu, S.W.3
  • 67
    • 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
  • 68
    • 1642456636 scopus 로고    scopus 로고
    • Characterization and analysis of thermal denaturation of antibodies by size exclusion high-performance liquid chromatography with quadruple detection
    • Hartmann WK, Saptharishi N, Yang XY, Mitra G, Soman G. 2004. Characterization and analysis of thermal denaturation of antibodies by size exclusion high-performance liquid chromatography with quadruple detection. Anal Biochem 325:227-239.
    • (2004) Anal Biochem , vol.325 , pp. 227-239
    • Hartmann, W.K.1    Saptharishi, N.2    Yang, X.Y.3    Mitra, G.4    Soman, G.5
  • 69
    • 32644461200 scopus 로고    scopus 로고
    • Loss of secreted antibody from transgenic plant tissue cultures due to surface adsorption
    • Doran PM. 2006. Loss of secreted antibody from transgenic plant tissue cultures due to surface adsorption. J Biotechnol 122:39-54.
    • (2006) J Biotechnol , vol.122 , pp. 39-54
    • Doran, P.M.1
  • 71
    • 0032962882 scopus 로고    scopus 로고
    • The effect of formulation excipients on protein stability and aerosol performance of spray-dried powders of a recombinant humanized anti-IgE monoclonal antibody
    • Andya JD, Maa YF, Costantino HR, Nguyen PA, Dasovich N, Sweeney TD, Hsu CC, Shire SJ. 1999. The effect of formulation excipients on protein stability and aerosol performance of spray-dried powders of a recombinant humanized anti-IgE monoclonal antibody. Pharm Res 16:350-358.
    • (1999) Pharm Res , vol.16 , pp. 350-358
    • Andya, J.D.1    Maa, Y.F.2    Costantino, H.R.3    Nguyen, P.A.4    Dasovich, N.5    Sweeney, T.D.6    Hsu, C.C.7    Shire, S.J.8
  • 72
    • 0030176302 scopus 로고    scopus 로고
    • Effect of pH, hydrogen peroxide and temperature on the stability of human monoclonal antibody
    • 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.
    • (1996) J Pharm Biomed Anal , vol.14 , pp. 1133-1140
    • Usami, A.1    Ohtsu, A.2    Takahama, S.3    Fujii, T.4
  • 73
    • 0027791511 scopus 로고
    • Orthoclone OKT3 chemical mechanims and functional effects of degradation of a therapeutic monoclonal antibody
    • Pearlman R, Wan YJ, editors, New York: Plenum Press, p
    • Rao PE, Kroon DJ. 1993. Orthoclone OKT3 chemical mechanims and functional effects of degradation of a therapeutic monoclonal antibody. In: Pearlman R, Wan YJ, editors. Stability and characterization of protein and peptide drugs case histories. New York: Plenum Press, p. 135-158.
    • (1993) Stability and characterization of protein and peptide drugs case histories , pp. 135-158
    • Rao, P.E.1    Kroon, D.J.2
  • 75
    • 0027729733 scopus 로고
    • The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation
    • Cleland JL, Powell MF, Shire SJ. 1993. The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation. Crit Rev Ther Drug Carrier Syst 10:307-377.
    • (1993) Crit Rev Ther Drug Carrier Syst , vol.10 , pp. 307-377
    • Cleland, J.L.1    Powell, M.F.2    Shire, S.J.3
  • 76
    • 0032904703 scopus 로고    scopus 로고
    • Secondary structure and protein deamidation
    • Xie M, Schowen RL. 1999. Secondary structure and protein deamidation. J Pharm Sci 88:8-13.
    • (1999) J Pharm Sci , vol.88 , pp. 8-13
    • Xie, M.1    Schowen, R.L.2
  • 77
    • 0028180406 scopus 로고
    • Identification of succinimide sites in proteins by N-terminal sequence analysis after alkaline hydroxylamine cleavage
    • Kwong MY, Harris RJ. 1994. Identification of succinimide sites in proteins by N-terminal sequence analysis after alkaline hydroxylamine cleavage. Protein Sci 3:147-149.
    • (1994) Protein Sci , vol.3 , pp. 147-149
    • Kwong, M.Y.1    Harris, R.J.2
  • 78
    • 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. 2005. Influence of pH, buffer species, and storage temperature on physicochemical stability of a humanized monoclonal antibody LA298. Int J Pharm 308:46-51.
    • (2005) Int J Pharm , vol.308 , pp. 46-51
    • Zheng, J.Y.1    Janis, L.J.2
  • 79
    • 0025788030 scopus 로고
    • Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides
    • Tyler-Cross R, Schirch V. 1991. Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides. J Biol Chem 266:22549-22556.
    • (1991) J Biol Chem , vol.266 , pp. 22549-22556
    • Tyler-Cross, R.1    Schirch, V.2
  • 81
    • 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 86:1250-1255.
    • (1997) J Pharm Sci , vol.86 , pp. 1250-1255
    • Lam, X.M.1    Yang, J.Y.2    Cleland, J.L.3
  • 82
    • 0029017877 scopus 로고
    • Processing of C-terminal lysine and arginine residues of proteins isolated from mammalian cell culture
    • Harris RJ. 1995. Processing of C-terminal lysine and arginine residues of proteins isolated from mammalian cell culture. J Chromatogr A 705:129-134.
    • (1995) J Chromatogr A , vol.705 , pp. 129-134
    • Harris, R.J.1
  • 83
    • 0344917507 scopus 로고    scopus 로고
    • A compendium and hydropathy/flexibility analysis of common reactive sites in proteins: Reactivity at Asn, Asp, Gln, and Met motifs in neutral pH solution
    • Pearlman R, Wang YJ, editors, New York: Plenum Press. p
    • Powell MF. 1996. A compendium and hydropathy/flexibility analysis of common reactive sites in proteins: Reactivity at Asn, Asp, Gln, and Met motifs in neutral pH solution. In: Pearlman R, Wang YJ, editors. Formulation, characterization, and stability of protein drugs. New York: Plenum Press. p. 1-140.
    • (1996) Formulation, characterization, and stability of protein drugs , pp. 1-140
    • Powell, M.F.1
  • 84
    • 85030524668 scopus 로고    scopus 로고
    • Stable intravenously-administrable immune globulin preparation. Baxter International Inc.,
    • US patent US5945098
    • Sarno MEC, Vasquez RA, Yung S-G, Graf CR. 1999. Stable intravenously-administrable immune globulin preparation. Baxter International Inc., US patent US5945098.
    • (1999)
    • Sarno, M.E.C.1    Vasquez, R.A.2    Yung, S.-G.3    Graf, C.R.4
  • 86
    • 0027960596 scopus 로고
    • Glycation of monoclonal antibodies impairs their ability to bind antigen
    • Kennedy DM, Skillen AW, Self CH. 1994. Glycation of monoclonal antibodies impairs their ability to bind antigen. Clin Exp Immunol 98:245-251.
    • (1994) Clin Exp Immunol , vol.98 , pp. 245-251
    • Kennedy, D.M.1    Skillen, A.W.2    Self, C.H.3
  • 87
    • 0042526640 scopus 로고    scopus 로고
    • The immunogenicity of biopharmaceuticals. Lessons learned and consequences for protein drug development
    • Patten PA, Schellekens H. 2003. The immunogenicity of biopharmaceuticals. Lessons learned and consequences for protein drug development. Dev Biol (Basel) 112:81-97.
    • (2003) Dev Biol (Basel) , vol.112 , pp. 81-97
    • Patten, P.A.1    Schellekens, H.2
  • 88
    • 27644477360 scopus 로고    scopus 로고
    • Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution
    • Liu J, Nguyen MD, Andya JD, Shire SJ. 2005. Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution. J Pharm Sci 94:1928-1940.
    • (2005) J Pharm Sci , vol.94 , pp. 1928-1940
    • Liu, J.1    Nguyen, M.D.2    Andya, J.D.3    Shire, S.J.4
  • 89
    • 3242798849 scopus 로고    scopus 로고
    • A simple method for improving protein solubility and long-term stability
    • Golovanov AP, Hautbergue GM, Wilson SA, Lian LY. 2004. A simple method for improving protein solubility and long-term stability. J Am Chem Soc 126:8933-8939.
    • (2004) J Am Chem Soc , vol.126 , pp. 8933-8939
    • Golovanov, A.P.1    Hautbergue, G.M.2    Wilson, S.A.3    Lian, L.Y.4
  • 92
    • 0036111474 scopus 로고    scopus 로고
    • Inverse relationship of protein concentration and aggregation
    • Treuheit MJ, Kosky AA, Brems DN. 2002. Inverse relationship of protein concentration and aggregation. Pharm Res 19:511-516.
    • (2002) Pharm Res , vol.19 , pp. 511-516
    • Treuheit, M.J.1    Kosky, A.A.2    Brems, D.N.3
  • 93
    • 0036784668 scopus 로고    scopus 로고
    • Peroxide formation in polysorbate 80 and protein stability
    • Ha E, Wang W, Wang YJ. 2002. Peroxide formation in polysorbate 80 and protein stability. J Pharm Sci 91:2252-2264.
    • (2002) J Pharm Sci , vol.91 , pp. 2252-2264
    • Ha, E.1    Wang, W.2    Wang, Y.J.3
  • 94
    • 0347300798 scopus 로고    scopus 로고
    • Development of a multidose formulation for a humanized monoclonal antibody using experimental design techniques
    • Gupta S, Kaisheva E. 2003. Development of a multidose formulation for a humanized monoclonal antibody using experimental design techniques. AAPS PharmSci 5:E8.
    • (2003) AAPS PharmSci , vol.5
    • Gupta, S.1    Kaisheva, E.2
  • 95
    • 0037285769 scopus 로고    scopus 로고
    • The influence of complexing agent and proteins on the corrosion of stainless steels and their metal components
    • Kocijan A, Milosev I, Pihlar B. 2003. The influence of complexing agent and proteins on the corrosion of stainless steels and their metal components. J Mater Sci Mater Med 14:69-77.
    • (2003) J Mater Sci Mater Med , vol.14 , pp. 69-77
    • Kocijan, A.1    Milosev, I.2    Pihlar, B.3
  • 96
    • 9644287860 scopus 로고    scopus 로고
    • Small changes, big effects in biological manufacturing
    • McCormick D. 2004. Small changes, big effects in biological manufacturing. Pharm Technol 28:16.
    • (2004) Pharm Technol , vol.28 , pp. 16
    • McCormick, D.1
  • 97
    • 0030770631 scopus 로고    scopus 로고
    • Rational design of stable lyophilized protein formulations: Some practical advice
    • Carpenter JF, Pikal MJ, Chang BS, Randolph TW. 1997. Rational design of stable lyophilized protein formulations: Some practical advice. Pharm Res 14:969-975.
    • (1997) Pharm Res , vol.14 , pp. 969-975
    • Carpenter, J.F.1    Pikal, M.J.2    Chang, B.S.3    Randolph, T.W.4
  • 98
    • 0034255393 scopus 로고    scopus 로고
    • Lyophilization and development of solid protein pharmaceuticals
    • Wang W. 2000. Lyophilization and development of solid protein pharmaceuticals. Int J Pharm 203:1-60.
    • (2000) Int J Pharm , vol.203 , pp. 1-60
    • Wang, W.1
  • 100
    • 0036366238 scopus 로고    scopus 로고
    • Practical approaches to protein formulation development
    • Chang BS, Hershenson S. 2002. Practical approaches to protein formulation development. Pharm Biotechnol 13:1-25.
    • (2002) Pharm Biotechnol , vol.13 , pp. 1-25
    • Chang, B.S.1    Hershenson, S.2
  • 101
    • 23844447975 scopus 로고    scopus 로고
    • Mechanism of protein stabilization by sugars during freeze-drying and storage: Native structure preservation, specific interaction, and/or immobilization in a glassy matrix?
    • Chang LL, Shepherd D, Sun J, Ouellette D, Grant KL, Tang XC, Pikal MJ. 2005. Mechanism of protein stabilization by sugars during freeze-drying and storage: Native structure preservation, specific interaction, and/or immobilization in a glassy matrix? J Pharm Sci 94:1427-1444.
    • (2005) J Pharm Sci , vol.94 , pp. 1427-1444
    • Chang, L.L.1    Shepherd, D.2    Sun, J.3    Ouellette, D.4    Grant, K.L.5    Tang, X.C.6    Pikal, M.J.7
  • 102
    • 23844461800 scopus 로고    scopus 로고
    • Effect of sorbitol and residual moisture on the stability of lyophilized antibodies: Implications for the mechanism of protein stabilization in the solid state
    • Chang LL, Shepherd D, Sun J, Tang XC, Pikal MJ. 2005. Effect of sorbitol and residual moisture on the stability of lyophilized antibodies: Implications for the mechanism of protein stabilization in the solid state. J Pharm Sci 94:1445-1455.
    • (2005) J Pharm Sci , vol.94 , pp. 1445-1455
    • Chang, L.L.1    Shepherd, D.2    Sun, J.3    Tang, X.C.4    Pikal, M.J.5
  • 103
    • 0030831389 scopus 로고    scopus 로고
    • The stability of insulin in crystalline and amorphous solids: Observation of greater stability for the amorphous form
    • Pikal MJ, Rigsbee DR. 1997. The stability of insulin in crystalline and amorphous solids: Observation of greater stability for the amorphous form. Pharm Res 14:1379-1387.
    • (1997) Pharm Res , vol.14 , pp. 1379-1387
    • Pikal, M.J.1    Rigsbee, D.R.2
  • 104
    • 0002469071 scopus 로고
    • Preserving dry biomaterials: The water replacement hypothesis, part 1
    • Crowe JH, Crowe LM, Carpenter JF. 1993. Preserving dry biomaterials: The water replacement hypothesis, part 1. Biopharm 6:28-37.
    • (1993) Biopharm , vol.6 , pp. 28-37
    • Crowe, J.H.1    Crowe, L.M.2    Carpenter, J.F.3
  • 105
    • 0002469071 scopus 로고
    • Preserving dry biomaterials: The water replacement hypothesis, part 2
    • Crowe JH, Crowe LM, Carpenter JF. 1993. Preserving dry biomaterials: The water replacement hypothesis, part 2. Biopharm 6:40-43.
    • (1993) Biopharm , vol.6 , pp. 40-43
    • Crowe, J.H.1    Crowe, L.M.2    Carpenter, J.F.3
  • 108
    • 0034954471 scopus 로고    scopus 로고
    • Characterization of murine monoclonal antibody to tumor necrosis factor (TNF-MAb) formulation for freeze drying cycle development
    • Ma X, Wang DQ, Bouffard R, MacKenzie A. 2001. Characterization of murine monoclonal antibody to tumor necrosis factor (TNF-MAb) formulation for freeze drying cycle development. Pharm Res 18:196-202.
    • (2001) Pharm Res , vol.18 , pp. 196-202
    • Ma, X.1    Wang, D.Q.2    Bouffard, R.3    MacKenzie, A.4
  • 109
    • 0031393964 scopus 로고    scopus 로고
    • The effect of operating and formulation variables on the morphology of spray-dried protein particles
    • Maa YF, Costantino HR, Nguyen PA, Hsu CC. 1997. The effect of operating and formulation variables on the morphology of spray-dried protein particles. Pharm Dev Technol 2:213-223.
    • (1997) Pharm Dev Technol , vol.2 , pp. 213-223
    • Maa, Y.F.1    Costantino, H.R.2    Nguyen, P.A.3    Hsu, C.C.4
  • 110
    • 12344290280 scopus 로고    scopus 로고
    • Spray-drying of proteins: Effects of sorbitol and trehalose on aggregation and FT-IR amide I spectrum of an immunoglobulin G
    • Maury M, Murphy K, Kumar S, Mauerer A, Lee G. 2005. Spray-drying of proteins: Effects of sorbitol and trehalose on aggregation and FT-IR amide I spectrum of an immunoglobulin G. Eur J Pharm Biopharm 59:251-261.
    • (2005) Eur J Pharm Biopharm , vol.59 , pp. 251-261
    • Maury, M.1    Murphy, K.2    Kumar, S.3    Mauerer, A.4    Lee, G.5
  • 112
    • 0031473148 scopus 로고    scopus 로고
    • Pharmacokinetics and tissue distribution of cisplatin and conjugates of cisplatin with carboxymethyldextran and A5B7 monoclonal antibody in CD1 mice
    • McIntosh DP, Cooke RJ, McLachlan AJ, Daley-Yates PT, Rowland M. 1997. Pharmacokinetics and tissue distribution of cisplatin and conjugates of cisplatin with carboxymethyldextran and A5B7 monoclonal antibody in CD1 mice. J Pharm Sci 86:1478-1483.
    • (1997) J Pharm Sci , vol.86 , pp. 1478-1483
    • McIntosh, D.P.1    Cooke, R.J.2    McLachlan, A.J.3    Daley-Yates, P.T.4    Rowland, M.5
  • 113
    • 0030628658 scopus 로고    scopus 로고
    • Delivery of proteins from a controlled release injectable implant
    • Yewey GL, Duysen EG, Cox SM, Dunn RL. 1997. Delivery of proteins from a controlled release injectable implant. Pharm Biotechnol 10:93-117.
    • (1997) Pharm Biotechnol , vol.10 , pp. 93-117
    • Yewey, G.L.1    Duysen, E.G.2    Cox, S.M.3    Dunn, R.L.4
  • 115
    • 0041664969 scopus 로고    scopus 로고
    • Controlled release of anti-cocaine catalytic antibody from biodegradable polymer microspheres
    • Homayoun P, Mandal T, Landry D, Komiskey H. 2003. Controlled release of anti-cocaine catalytic antibody from biodegradable polymer microspheres. J Pharm Pharmacol 55:933-938.
    • (2003) J Pharm Pharmacol , vol.55 , pp. 933-938
    • Homayoun, P.1    Mandal, T.2    Landry, D.3    Komiskey, H.4


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