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Volumn 59, Issue 3, 2005, Pages 407-417

Induction and analysis of aggregates in a liquid IgG1-antibody formulation

Author keywords

Aggregation; Antibody; Association; Dynamic light scattering; Light obscuration; Mechanical stress; Protein stability; Turbidity

Indexed keywords

IMMUNOGLOBULIN G ANTIBODY; POLYSORBATE 80; SURFACTANT;

EID: 14844334231     PISSN: 09396411     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejpb.2004.12.004     Document Type: Article
Times cited : (284)

References (52)
  • 2
    • 0027729733 scopus 로고
    • The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation
    • J.L. Cleland, M.F. Powell, and S.J. Shire The development of stable protein formulations: a close look at protein aggregation, deamidation, and oxidation Crit. Rev. Ther. Drug Carrier Syst. 10 1993 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
  • 4
    • 0032782071 scopus 로고    scopus 로고
    • Instability, stabilization, and formulation of liquid protein pharmaceuticals
    • W. Wang Instability, stabilization, and formulation of liquid protein pharmaceuticals Int. J. Pharm. 185 1999 129 188
    • (1999) Int. J. Pharm. , vol.185 , pp. 129-188
    • Wang, W.1
  • 5
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a partially folded intermediate in alpha-synuclein fibril formation
    • V.N. Uversky, J. Li, and A.L. Fink Evidence for a partially folded intermediate in alpha-synuclein fibril formation J. Biol. Chem. 276 2001 10737 10744
    • (2001) J. Biol. Chem. , vol.276 , pp. 10737-10744
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 6
    • 0029993064 scopus 로고    scopus 로고
    • Simulations of reversible protein aggregate and crystal structure
    • S.Y. Patro, and T.M. Przybycien Simulations of reversible protein aggregate and crystal structure Biophys. J. 70 1996 2888 2992
    • (1996) Biophys. J. , vol.70 , pp. 2888-2992
    • Patro, S.Y.1    Przybycien, T.M.2
  • 8
    • 0001690963 scopus 로고
    • Separation of solids in the surface-layers of solutions and suspension (observations on surface-membranes, bubbles, emulsions and mechanical coagulation)
    • W. Ramsden Separation of solids in the surface-layers of solutions and suspension (observations on surface-membranes, bubbles, emulsions and mechanical coagulation) Proc. Roy. Soc. Lond. 72 1904 156 164
    • (1904) Proc. Roy. Soc. Lond. , vol.72 , pp. 156-164
    • Ramsden, W.1
  • 9
    • 0036598634 scopus 로고    scopus 로고
    • Bioequivalence and the immunogenicity of biopharmaceuticals
    • H. Schellekens Bioequivalence and the immunogenicity of biopharmaceuticals Nat. Rev. Drug Discov. 1 2002 457 462
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 457-462
    • Schellekens, H.1
  • 11
    • 0026004620 scopus 로고
    • Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces
    • V. Sluzky, J.A. Tamada, A.M. Klibanov, and R. Langer Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces PNAS 88 1991 9377 9381
    • (1991) PNAS , vol.88 , pp. 9377-9381
    • Sluzky, V.1    Tamada, J.A.2    Klibanov, A.M.3    Langer, R.4
  • 13
    • 0342762048 scopus 로고    scopus 로고
    • Protein denaturation by combined effect of shear and air-liquid interface
    • Y.-F. Maa, and C.C. Hsu Protein denaturation by combined effect of shear and air-liquid interface Biotechnol. Bioeng. 54 1997 503 512
    • (1997) Biotechnol. Bioeng. , vol.54 , pp. 503-512
    • Maa, Y.-F.1    Hsu, C.C.2
  • 14
    • 9544258376 scopus 로고    scopus 로고
    • Effect of high shear on proteins
    • Y.-F. Maa, and C.C. Hsu Effect of high shear on proteins Biotechnol. Bioeng. 51 1996 458 465
    • (1996) Biotechnol. Bioeng. , vol.51 , pp. 458-465
    • Maa, Y.-F.1    Hsu, C.C.2
  • 15
    • 0027228385 scopus 로고
    • Techniques for assessing the effects of pharmaceutical excipients on the aggregation of porcine growth hormone
    • S.A. Charman, K.L. Mason, and W.N. Charman Techniques for assessing the effects of pharmaceutical excipients on the aggregation of porcine growth hormone Pharm. Res. 10 1993 954 962
    • (1993) Pharm. Res. , vol.10 , pp. 954-962
    • Charman, S.A.1    Mason, K.L.2    Charman, W.N.3
  • 16
    • 0031391073 scopus 로고    scopus 로고
    • Use of poloxamer polymers to stabilize recombinant human growth hormone against various processing stresses
    • M. Katakam, and A.K. Banga Use of poloxamer polymers to stabilize recombinant human growth hormone against various processing stresses Pharm. Dev. Technol. 2 1997 143 149
    • (1997) Pharm. Dev. Technol. , vol.2 , pp. 143-149
    • Katakam, M.1    Banga, A.K.2
  • 17
    • 0029074530 scopus 로고
    • Effect of surfactants on the physical stability of recombinant human growth hormone
    • M. Katakam, L.N. Bell, and A.K. Banga Effect of surfactants on the physical stability of recombinant human growth hormone J. Pharm. Sci. 84 1995 713 716
    • (1995) J. Pharm. Sci. , vol.84 , pp. 713-716
    • Katakam, M.1    Bell, L.N.2    Banga, A.K.3
  • 19
    • 0034285187 scopus 로고    scopus 로고
    • Static and dynamic light scattering from aggregating particles
    • V.A. Bloomfield Static and dynamic light scattering from aggregating particles Biopolymers 54 2000 168 172
    • (2000) Biopolymers , vol.54 , pp. 168-172
    • Bloomfield, V.A.1
  • 21
    • 0025671869 scopus 로고
    • Refolding and aggregation of bovine carbonic anhydrase B: Quasi-elastic light scattering analysis
    • J.L. Cleland, and D.I. Wang Refolding and aggregation of bovine carbonic anhydrase B: quasi-elastic light scattering analysis Biochemistry 29 1990 11072 11078
    • (1990) Biochemistry , vol.29 , pp. 11072-11078
    • Cleland, J.L.1    Wang, D.I.2
  • 22
    • 0028126885 scopus 로고
    • Stability of rhbFGF as determined by UV spectroscopic measurements of turbidity
    • G.A. Eberlein, P.R. Stratton, and Y.J. Wang Stability of rhbFGF as determined by UV spectroscopic measurements of turbidity PDA J. Pharm. Sci. Technol. 48 1994 224 230
    • (1994) PDA J. Pharm. Sci. Technol. , vol.48 , pp. 224-230
    • Eberlein, G.A.1    Stratton, P.R.2    Wang, Y.J.3
  • 24
    • 0017603553 scopus 로고
    • Scattering correction to the absorbance, wavelength dependence of the refractive index increment, and molecular weight of the bovine liver glutamate dehydrogenase oligomer and subunits
    • H. Eisenberg, R. Josephs, and E. Reisler Scattering correction to the absorbance, wavelength dependence of the refractive index increment, and molecular weight of the bovine liver glutamate dehydrogenase oligomer and subunits Biopolymers 16 1977 2773 2783
    • (1977) Biopolymers , vol.16 , pp. 2773-2783
    • Eisenberg, H.1    Josephs, R.2    Reisler, E.3
  • 25
    • 0031436270 scopus 로고    scopus 로고
    • Classical light scattering quantitation of protein aggregates: Off-line spectroscopy versus HPLC detection
    • M. Kunitani, S. Wolfe, S. Rana, C. Apicella, V. Levi, and G. Dollinger Classical light scattering quantitation of protein aggregates: off-line spectroscopy versus HPLC detection J. Pharm. Biomed. Anal. 16 1997 573 586
    • (1997) J. Pharm. Biomed. Anal. , vol.16 , pp. 573-586
    • Kunitani, M.1    Wolfe, S.2    Rana, S.3    Apicella, C.4    Levi, V.5    Dollinger, G.6
  • 26
    • 0026238663 scopus 로고
    • Heat aggregation studies of phycobilisomes, ferritin, insulin and immunoglobulin by dynamic light scattering
    • B.P. Singh, H.B. Bohidar, and S. Chopra Heat aggregation studies of phycobilisomes, ferritin, insulin and immunoglobulin by dynamic light scattering Biopolymers 31 1991 1387 1396
    • (1991) Biopolymers , vol.31 , pp. 1387-1396
    • Singh, B.P.1    Bohidar, H.B.2    Chopra, S.3
  • 27
    • 0345876459 scopus 로고    scopus 로고
    • Surfactant-stabilized protein formulations: A review of protein-surfactant interactions and novel analytical methodologies
    • L.S. Jones, N.B. Bam, and T.W. Randolph Surfactant-stabilized protein formulations: a review of protein-surfactant interactions and novel analytical methodologies ACS Symp. Ser. 675 1997 206 222
    • (1997) ACS Symp. Ser. , vol.675 , pp. 206-222
    • Jones, L.S.1    Bam, N.B.2    Randolph, T.W.3
  • 28
    • 0037177491 scopus 로고    scopus 로고
    • Protection mechanism of Tween 80 during freeze-thawing of a model protein, LDH
    • A. Hillgren, J. Lindgren, and M. Alden Protection mechanism of Tween 80 during freeze-thawing of a model protein, LDH Int. J. Pharm. 237 2002 57 69
    • (2002) Int. J. Pharm. , vol.237 , pp. 57-69
    • Hillgren, A.1    Lindgren, J.2    Alden, M.3
  • 29
    • 0031660957 scopus 로고    scopus 로고
    • Effects of Tween 80 and sucrose on acute short-term stability and long-term storage at -20 degrees C of a recombinant hemoglobin
    • B.A. Kerwin, M.C. Heller, S.H. Levin, and T.W. Randolph Effects of Tween 80 and sucrose on acute short-term stability and long-term storage at -20 degrees C of a recombinant hemoglobin J. Pharm. Sci. 87 1998 1062 1068
    • (1998) J. Pharm. Sci. , vol.87 , pp. 1062-1068
    • Kerwin, B.A.1    Heller, M.C.2    Levin, S.H.3    Randolph, T.W.4
  • 30
    • 0030443567 scopus 로고    scopus 로고
    • Surface-induced denaturation of proteins during freezing and its inhibition by surfactants
    • B.S. Chang, B.S. Kendrick, and J.F. Carpenter Surface-induced denaturation of proteins during freezing and its inhibition by surfactants J. Pharm. Sci. 85 1996 1325 1330
    • (1996) J. Pharm. Sci. , vol.85 , pp. 1325-1330
    • Chang, B.S.1    Kendrick, B.S.2    Carpenter, J.F.3
  • 31
    • 0031742802 scopus 로고    scopus 로고
    • Tween protects recombinant human growth hormone against agitation-induced damage via hydrophobic interactions
    • N.B. Bam, J.L. Cleland, J. Yang, M.C. Manning, J.F. Carpenter, R.F. Kelley, and T.W. Randolph Tween protects recombinant human growth hormone against agitation-induced damage via hydrophobic interactions J. Pharm. Sci. 87 1998 1554 1559
    • (1998) J. Pharm. Sci. , vol.87 , pp. 1554-1559
    • Bam, N.B.1    Cleland, J.L.2    Yang, J.3    Manning, M.C.4    Carpenter, J.F.5    Kelley, R.F.6    Randolph, T.W.7
  • 35
    • 0030292616 scopus 로고    scopus 로고
    • Molten globule intermediate of recombinant human growth hormone: Stabilization with surfactants
    • N.B. Bam, J.L. Cleland, and T.W. Randolph Molten globule intermediate of recombinant human growth hormone: stabilization with surfactants Biotechnol. Prog. 12 1996 801 809
    • (1996) Biotechnol. Prog. , vol.12 , pp. 801-809
    • Bam, N.B.1    Cleland, J.L.2    Randolph, T.W.3
  • 36
    • 0023255917 scopus 로고
    • Detergent-assisted refolding of guanidinium chloride-denatured rhodanese the effects of the concentration and type of detergent
    • S. Tandon, and P.M. Horowitz Detergent-assisted refolding of guanidinium chloride-denatured rhodanese The effects of the concentration and type of detergent J. Biol. Chem. 262 1987 4486 4491
    • (1987) J. Biol. Chem. , vol.262 , pp. 4486-4491
    • Tandon, S.1    Horowitz, P.M.2
  • 37
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • N. Timasheff The control of protein stability and association by weak interactions with water: how do solvents affect these processes? Annu. Rev. Biophys. Biomol. Struct. 22 1993 67 97
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 67-97
    • Timasheff, N.1
  • 38
    • 0016657917 scopus 로고
    • Solubilization of membranes by detergents
    • A. Helenius, and K. Simons Solubilization of membranes by detergents Biochim. Biophys. Acta 415 1975 29 79
    • (1975) Biochim. Biophys. Acta , vol.415 , pp. 29-79
    • Helenius, A.1    Simons, K.2
  • 39
    • 14844289396 scopus 로고    scopus 로고
    • Particulate contamination: Sub-visible particles
    • Particulate contamination: sub-visible particles, European Pharmacopoeia, 2002, pp. 2915-2918.
    • (2002) European Pharmacopoeia , pp. 2915-2918
  • 40
    • 14844308908 scopus 로고    scopus 로고
    • Particulate matter in injections
    • Particulate matter in injections, United States Pharmacopeia, 2003, pp. 2189-2196.
    • (2003) United States Pharmacopeia , pp. 2189-2196
  • 41
    • 0030913488 scopus 로고    scopus 로고
    • Particulate matter determination in LVPs produced in Dutch hospital pharmacies Part 1: Particle-counting accuracy
    • J. Van der Veen, P. Verbrugge, F.J. Van de Vaart, and F.A. Boom Particulate matter determination in LVPs produced in Dutch hospital pharmacies Part 1: Particle-counting accuracy PDA J. Pharm. Sci. Technol. 51 1997 81 88
    • (1997) PDA J. Pharm. Sci. Technol. , vol.51 , pp. 81-88
    • Van Der Veen, J.1    Verbrugge, P.2    Van De Vaart, F.J.3    Boom, F.A.4
  • 42
    • 1642452167 scopus 로고    scopus 로고
    • Clarity and degree of opalescense of liquids
    • Clarity and degree of opalescense of liquids, European Pharmacopoeia, 2002, pp. 23-23.
    • (2002) European Pharmacopoeia , pp. 23-23
  • 43
    • 0025793265 scopus 로고
    • The effects of formulation variables on the stability of freeze-dried human growth hormone
    • M.J. Pikal, K.M. Dellerman, M.L. Roy, and R.M. Riggin The effects of formulation variables on the stability of freeze-dried human growth hormone Pharm. Res. 8 1991 427 436
    • (1991) Pharm. Res. , vol.8 , pp. 427-436
    • Pikal, M.J.1    Dellerman, K.M.2    Roy, M.L.3    Riggin, R.M.4
  • 44
    • 0014995599 scopus 로고
    • Correction of light-scattering errors in spectrophotometric protein determinations
    • A.F.G. Winder, and W.L.G. Gent Correction of light-scattering errors in spectrophotometric protein determinations Biopolymers 10 1971 1243 1251
    • (1971) Biopolymers , vol.10 , pp. 1243-1251
    • Winder, A.F.G.1    Gent, W.L.G.2
  • 46
    • 0000007267 scopus 로고
    • Characterization of proteins during aggregation using turbidimetry
    • L.H. Garcia-Rubio Characterization of proteins during aggregation using turbidimetry Chem. Eng. Commun. 80 1989 193 210
    • (1989) Chem. Eng. Commun. , vol.80 , pp. 193-210
    • Garcia-Rubio, L.H.1
  • 48
    • 19244375608 scopus 로고    scopus 로고
    • Influence of heavy metal ions on antibodies and immune complexes investigated by dynamic light scattering and enzyme-linked immunosorbent assay
    • R. Bauer, A. Müller, M. Richter, K. Schneider, J. Frey, and W. Engelhardt Influence of heavy metal ions on antibodies and immune complexes investigated by dynamic light scattering and enzyme-linked immunosorbent assay Biochim. Biophys. Acta 1334 1997 98 108
    • (1997) Biochim. Biophys. Acta , vol.1334 , pp. 98-108
    • Bauer, R.1    Müller, A.2    Richter, M.3    Schneider, K.4    Frey, J.5    Engelhardt, W.6
  • 49
    • 0346502228 scopus 로고    scopus 로고
    • Characterization methods for the physical stability of biopharmaceuticals
    • L.T. Nguyen, J.M. Wiencek, and L.E. Kirsch Characterization methods for the physical stability of biopharmaceuticals PDA J. Pharm. Sci. Technol. 57 2003 429 445
    • (2003) PDA J. Pharm. Sci. Technol. , vol.57 , pp. 429-445
    • Nguyen, L.T.1    Wiencek, J.M.2    Kirsch, L.E.3
  • 50
    • 85039992513 scopus 로고    scopus 로고
    • Q1A(R2): Stability testing of new drug substances and products
    • Q1A(R2): Stability testing of new drug substances and products. International conference on harmonisation, 2003, 1-15.
    • (2003) International Conference on Harmonisation , pp. 1-15
  • 51
    • 85030814463 scopus 로고    scopus 로고
    • PhD thesis, in preparation.
    • K. Schimanski, PhD thesis, in preparation.
    • Schimanski, K.1
  • 52
    • 85030807352 scopus 로고    scopus 로고
    • PhD thesis, Untersuchungen zum Einfrier- und Auftauverhalten pharmazeutischer Humanproteinlösungen im Großmaßstab, Munich
    • R. Zippelius, PhD thesis, Untersuchungen zum Einfrier- und Auftauverhalten pharmazeutischer Humanproteinlösungen im Großmaßstab, Munich, 2002.
    • (2002)
    • Zippelius, R.1


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