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Volumn 105, Issue 8, 2016, Pages 2310-2318

Characterizing Reversible Protein Association at Moderately High Concentration Via Composition-Gradient Static Light Scattering

Author keywords

biopharmaceuticals characterization; biotechnology; light scattering; protein aggregation; protein formulation; stability

Indexed keywords

BINDING AFFINITY; BIOTECHNOLOGY; EXPECTATION; PHOTON CORRELATION SPECTROSCOPY; PROTEIN AGGREGATION; SEDIMENTATION; STOICHIOMETRY; CHEMICAL MODEL; CHEMISTRY; LIGHT; PHARMACEUTICS; PROCEDURES; PROTEIN MULTIMERIZATION; RADIATION SCATTERING; SOLUTION AND SOLUBILITY; THERMODYNAMICS;

EID: 84978997518     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1016/j.xphs.2016.05.018     Document Type: Article
Times cited : (8)

References (16)
  • 1
    • 11844292073 scopus 로고    scopus 로고
    • New methods for measuring macromolecular interactions in solution via static light scattering: basic methodology and application to nonassociating and self-associating proteins
    • 1 Attri, A.K., Minton, A.P., New methods for measuring macromolecular interactions in solution via static light scattering: basic methodology and application to nonassociating and self-associating proteins. Anal Biochem 337 (2005), 103–110.
    • (2005) Anal Biochem , vol.337 , pp. 103-110
    • Attri, A.K.1    Minton, A.P.2
  • 2
    • 33645984885 scopus 로고    scopus 로고
    • Rapid quantitative characterization of protein interactions by composition gradient static light scattering
    • 2 Kameyama, K., Minton, A.P., Rapid quantitative characterization of protein interactions by composition gradient static light scattering. Biophys J 90 (2006), 2164–2169.
    • (2006) Biophys J , vol.90 , pp. 2164-2169
    • Kameyama, K.1    Minton, A.P.2
  • 3
    • 84877067922 scopus 로고    scopus 로고
    • Light-scattering-based analysis of biomolecular interactions
    • and references therein
    • 3 Some, D., Light-scattering-based analysis of biomolecular interactions. Biophys Rev 5 (2013), 147–158 and references therein.
    • (2013) Biophys Rev , vol.5 , pp. 147-158
    • Some, D.1
  • 4
    • 0002628768 scopus 로고
    • Light scattering in multi-component systems
    • 4 Stockmayer, W.H., Light scattering in multi-component systems. J Chem Phys 18 (1950), 58–61.
    • (1950) J Chem Phys , vol.18 , pp. 58-61
    • Stockmayer, W.H.1
  • 5
    • 84985721961 scopus 로고
    • Light scattering of bovine serum albumin solutions: extension of the hard particle model to allow for electrostatic repulsion
    • 5 Minton, A.P., Edelhoch, H., Light scattering of bovine serum albumin solutions: extension of the hard particle model to allow for electrostatic repulsion. Biopolymers 21 (1982), 451–459.
    • (1982) Biopolymers , vol.21 , pp. 451-459
    • Minton, A.P.1    Edelhoch, H.2
  • 6
    • 0041931122 scopus 로고    scopus 로고
    • Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges
    • 6 Hall, D., Minton, A.P., Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges. Biochim Biophys Acta 1649 (2003), 127–139.
    • (2003) Biochim Biophys Acta , vol.1649 , pp. 127-139
    • Hall, D.1    Minton, A.P.2
  • 7
    • 0032311227 scopus 로고    scopus 로고
    • Molecular crowding: analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion
    • 7 Minton, A., Molecular crowding: analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion. Methods Enzymol 295 (1998), 127–149.
    • (1998) Methods Enzymol , vol.295 , pp. 127-149
    • Minton, A.1
  • 8
    • 0025700708 scopus 로고
    • Thermodynamic nonideality in macromolecular solutions
    • 8 Shearwin, K.E., Winzor, D.J., Thermodynamic nonideality in macromolecular solutions. Eur J Biochem 190 (1990), 523–529.
    • (1990) Eur J Biochem , vol.190 , pp. 523-529
    • Shearwin, K.E.1    Winzor, D.J.2
  • 9
    • 33645087051 scopus 로고
    • Statistical thermodynamics of convex molecule fluids
    • 9 Boublík, T., Statistical thermodynamics of convex molecule fluids. Mol Phys 27 (1974), 1415–1427.
    • (1974) Mol Phys , vol.27 , pp. 1415-1427
    • Boublík, T.1
  • 10
    • 0023322946 scopus 로고
    • Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. I. Self-associating proteins
    • 10 Chatelier, R.C., Minton, A.P., Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. I. Self-associating proteins. Biopolymers 26 (1987), 507–524.
    • (1987) Biopolymers , vol.26 , pp. 507-524
    • Chatelier, R.C.1    Minton, A.P.2
  • 11
    • 65549164345 scopus 로고    scopus 로고
    • Static light scattering from concentrated protein solutions II: experimental test of theory for protein mixtures and weakly self-associating proteins
    • 11 Fernández, C., Minton, A.P., Static light scattering from concentrated protein solutions II: experimental test of theory for protein mixtures and weakly self-associating proteins. Biophys J 96 (2009), 1992–1998.
    • (2009) Biophys J , vol.96 , pp. 1992-1998
    • Fernández, C.1    Minton, A.P.2
  • 12
    • 34447504216 scopus 로고    scopus 로고
    • Static light scattering from concentrated protein solutions, I: general theory for protein mixtures and application to self-associating proteins
    • 12 Minton, A.P., Static light scattering from concentrated protein solutions, I: general theory for protein mixtures and application to self-associating proteins. Biophys J 93 (2007), 1321–1328.
    • (2007) Biophys J , vol.93 , pp. 1321-1328
    • Minton, A.P.1
  • 13
    • 84922901105 scopus 로고    scopus 로고
    • Mechanism of reversible self-association of a monoclonal antibody: role of electrostatic and hydrophobic interactions
    • 13 Esfandiary, R., Parupudi, A., Casas-Finet, J., Gadre, D., Sathish, H., Mechanism of reversible self-association of a monoclonal antibody: role of electrostatic and hydrophobic interactions. J Pharm Sci 104 (2015), 577–586.
    • (2015) J Pharm Sci , vol.104 , pp. 577-586
    • Esfandiary, R.1    Parupudi, A.2    Casas-Finet, J.3    Gadre, D.4    Sathish, H.5
  • 14
    • 84881588643 scopus 로고    scopus 로고
    • A systematic multitechnique approach for detection and characterization of reversible self-association during formulation development of therapeutic antibodies
    • 14 Esfandiary, R., Hayes, D.B., Parupudi, A., et al. A systematic multitechnique approach for detection and characterization of reversible self-association during formulation development of therapeutic antibodies. J Pharm Sci 102 (2013), 3089–3099.
    • (2013) J Pharm Sci , vol.102 , pp. 3089-3099
    • Esfandiary, R.1    Hayes, D.B.2    Parupudi, A.3
  • 15
    • 77957843464 scopus 로고    scopus 로고
    • Intermolecular interactions of IgG1 monoclonal antibodies at high concentrations characterized by light scattering
    • 15 Scherer, T.M., Liu, J., Shire, S.J., Intermolecular interactions of IgG1 monoclonal antibodies at high concentrations characterized by light scattering. J Phys Chem B 114:40 (2010), 12948–12957.
    • (2010) J Phys Chem B , vol.114 , Issue.40 , pp. 12948-12957
    • Scherer, T.M.1    Liu, J.2    Shire, S.J.3
  • 16
    • 58149461402 scopus 로고    scopus 로고
    • Ion-specific modulation of protein interactions: anion-induced, reversible oligomerization of a fusion protein
    • 16 Gokarn, Y.R., Fesinmeyer, R.M., Saluja, A., et al. Ion-specific modulation of protein interactions: anion-induced, reversible oligomerization of a fusion protein. Protein Sci 18:1 (2009), 169–179.
    • (2009) Protein Sci , vol.18 , Issue.1 , pp. 169-179
    • Gokarn, Y.R.1    Fesinmeyer, R.M.2    Saluja, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.