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Volumn 472, Issue , 2015, Pages 7-20

Concomitant Raman spectroscopy and dynamic light scattering for characterization of therapeutic proteins at high concentrations

Author keywords

Aggregation; Antibody; Dynamic light scattering; Protein formulation; Protein stability; Raman spectroscopy

Indexed keywords

AGGLOMERATION; ANTIBODIES; DYNAMIC LIGHT SCATTERING; HYDRODYNAMICS; ISOTHERMS; RAMAN SPECTROSCOPY; SPECTROMETERS; STABILITY; THERMODYNAMIC STABILITY;

EID: 84921021627     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2014.11.016     Document Type: Article
Times cited : (93)

References (61)
  • 1
    • 84886072770 scopus 로고    scopus 로고
    • Approaches to control protein aggregation during bulk production
    • W. Wang, C.J. Roberts (Eds.), John Wiley, New York
    • L.O. Narhi, Y. Jiang, R. Deshpande, S. Kang, J. Shultz, Approaches to control protein aggregation during bulk production, in: W. Wang, C.J. Roberts (Eds.), Aggregation of Therapeutic Proteins, John Wiley, New York, 2010, pp. 257-299.
    • (2010) Aggregation of Therapeutic Proteins , pp. 257-299
    • Narhi, L.O.1    Jiang, Y.2    Deshpande, R.3    Kang, S.4    Shultz, J.5
  • 2
    • 84881028178 scopus 로고    scopus 로고
    • Effect of ionic strength and pH on the physical and chemical stability of a monoclonal antibody antigen-binding fragment
    • T. Wang, O.S. Kumru, L. Yi, Y.J. Wang, J. Zhang, J.H. Kim, S.B. Joshi, C.R. Middaugh, D.B. Volkin, Effect of ionic strength and pH on the physical and chemical stability of a monoclonal antibody antigen-binding fragment, J. Pharm. Sci. 102 (2013) 2520-2537.
    • (2013) J. Pharm. Sci. , vol.102 , pp. 2520-2537
    • Wang, T.1    Kumru, O.S.2    Yi, L.3    Wang, Y.J.4    Zhang, J.5    Kim, J.H.6    Joshi, S.B.7    Middaugh, C.R.8    Volkin, D.B.9
  • 3
    • 84878146591 scopus 로고    scopus 로고
    • Characterization and stabilization of recombinant human protein pentraxin (rhPTX-2), J
    • J. Liu, C.A. Blasie, S. Shi, S.B. Joshi, C.R. Middaugh, D.B. Volkin, Characterization and stabilization of recombinant human protein pentraxin (rhPTX-2), J. Pharm. Sci. 102 (2013) 827-841.
    • (2013) Pharm. Sci. , vol.102 , pp. 827-841
    • Liu, J.1    Blasie, C.A.2    Shi, S.3    Joshi, S.B.4    Middaugh, C.R.5    Volkin, D.B.6
  • 4
    • 84897951293 scopus 로고    scopus 로고
    • Protein comparability assessments and potential applicability of high throughput biophysical methods and data visualization tools to compare physical stability profiles
    • M.A. Alsenaidy, N.K. Jain, J.H. Kim, C.R. Middaugh, D.B. Volkin, Protein comparability assessments and potential applicability of high throughput biophysical methods and data visualization tools to compare physical stability profiles, Front. Pharmacol. 5 (2014) 39.
    • (2014) Front. Pharmacol. , vol.5 , pp. 39
    • Alsenaidy, M.A.1    Jain, N.K.2    Kim, J.H.3    Middaugh, C.R.4    Volkin, D.B.5
  • 5
    • 84877623789 scopus 로고    scopus 로고
    • Analytical lessons learned from selected therapeutic protein drug comparability studies
    • M. Federici, A. Lubiniecki, P. Manikwar, D.B. Volkin, Analytical lessons learned from selected therapeutic protein drug comparability studies, Biologicals 41 (2013) 131-147.
    • (2013) Biologicals , vol.41 , pp. 131-147
    • Federici, M.1    Lubiniecki, A.2    Manikwar, P.3    Volkin, D.B.4
  • 8
    • 69249206868 scopus 로고    scopus 로고
    • A critical review of methods for size characterization of nonparticulate protein aggregates
    • J.S. Philo, A critical review of methods for size characterization of nonparticulate protein aggregates, Curr. Pharm. Biotechnol. 10 (2009) 359-372.
    • (2009) Curr. Pharm. Biotechnol. , vol.10 , pp. 359-372
    • Philo, J.S.1
  • 9
    • 78650577461 scopus 로고    scopus 로고
    • Subvisible particle counting provides a sensitive method of detecting and quantifying aggregation of monoclonal antibody caused by freeze-thawing: Insights into the roles of particles in the protein aggregation pathway
    • J.G. Barnard, S. Singh, T.W. Randolph, J.F. Carpenter, Subvisible particle counting provides a sensitive method of detecting and quantifying aggregation of monoclonal antibody caused by freeze-thawing: insights into the roles of particles in the protein aggregation pathway, J. Pharm. Sci. 100 (2011) 492-503.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 492-503
    • Barnard, J.G.1    Singh, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 11
    • 84864115266 scopus 로고    scopus 로고
    • Monitoring of subvisible particles in therapeutic proteins
    • S.K. Singh, M.R. Toler, Monitoring of subvisible particles in therapeutic proteins, Methods Mol. Biol. 899 (2012) 379-401.
    • (2012) Methods Mol. Biol. , vol.899 , pp. 379-401
    • Singh, S.K.1    Toler, M.R.2
  • 12
    • 68949085124 scopus 로고    scopus 로고
    • Protein aggregation: Pathways, induction factors, and analysis
    • H.C. Mahler, W. Friess, U. Grauschopf, S. Kiese, Protein aggregation: pathways, induction factors, and analysis, J. Pharm. Sci. 98 (2009) 2909-2934.
    • (2009) J. Pharm. Sci. , vol.98 , pp. 2909-2934
    • Mahler, H.C.1    Friess, W.2    Grauschopf, U.3    Kiese, S.4
  • 13
    • 36849073223 scopus 로고    scopus 로고
    • Raman spectroscopy of protein pharmaceuticals
    • Z.Q. Wen, Raman spectroscopy of protein pharmaceuticals, J. Pharm. Sci. 96 (2007) 2861-2878.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 2861-2878
    • Wen, Z.Q.1
  • 14
    • 79958163072 scopus 로고    scopus 로고
    • Analysis of the mechanism of lysozyme pressure denaturation from Raman spectroscopy investigations, and comparison with thermal denaturation
    • A. Hedoux, Y. Guinet, L. Paccou, Analysis of the mechanism of lysozyme pressure denaturation from Raman spectroscopy investigations, and comparison with thermal denaturation, J. Phys. Chem. B 115 (2011) 6740-6748.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 6740-6748
    • Hedoux, A.1    Guinet, Y.2    Paccou, L.3
  • 15
    • 70350571211 scopus 로고    scopus 로고
    • Influence of metal ions on thermal aggregation of bovine serum albumin: Aggregation kinetics and structural changes
    • G. Navarra, A. Tinti, M. Leone, V. Militello, A. Torreggiani, Influence of metal ions on thermal aggregation of bovine serum albumin: aggregation kinetics and structural changes, J. Inorg. Biochem. 103 (2009) 1729-1738.
    • (2009) J. Inorg. Biochem. , vol.103 , pp. 1729-1738
    • Navarra, G.1    Tinti, A.2    Leone, M.3    Militello, V.4    Torreggiani, A.5
  • 16
    • 84875777934 scopus 로고    scopus 로고
    • Monitoring guanidinium-induced structural changes in ribonuclease proteins using Raman spectroscopy and 2D correlation analysis
    • V.L. Brewster, L. Ashton, R. Goodacre, Monitoring guanidinium-induced structural changes in ribonuclease proteins using Raman spectroscopy and 2D correlation analysis, Anal. Chem. 85 (2013) 3570-3575.
    • (2013) Anal. Chem. , vol.85 , pp. 3570-3575
    • Brewster, V.L.1    Ashton, L.2    Goodacre, R.3
  • 17
    • 1542299045 scopus 로고    scopus 로고
    • Raman spectroscopy of heat-induced fine-stranded and particulate β-lactoglobulin gels
    • S. Ikeda, E.C.Y. Li-Chan, Raman spectroscopy of heat-induced fine-stranded and particulate β-lactoglobulin gels, Food Hydrocolloids 18 (2004) 489-498.
    • (2004) Food Hydrocolloids , vol.18 , pp. 489-498
    • Ikeda, S.1    Li-Chan, E.C.Y.2
  • 18
    • 0031573469 scopus 로고    scopus 로고
    • Spectroscopic study of secondary structure and thermal denaturation of recombinant human factor XIII in aqueous solution
    • A.C. Dong, B. Kendrick, L. Kreilgard, J. Matsuura, M.C. Manning, J.F. Carpenter, Spectroscopic study of secondary structure and thermal denaturation of recombinant human factor XIII in aqueous solution, Arch. Biochem. Biophys. 347 (1997) 213-220.
    • (1997) Arch. Biochem. Biophys. , vol.347 , pp. 213-220
    • Dong, A.C.1    Kendrick, B.2    Kreilgard, L.3    Matsuura, J.4    Manning, M.C.5    Carpenter, J.F.6
  • 19
    • 81155122975 scopus 로고    scopus 로고
    • Impact of short range hydrophobic interactions and long range electrostatic forces on the aggregation kinetics of a monoclonal antibody and a dual-variable domain immunoglobulin at low and high concentrations
    • V. Kumar, N. Dixit, L.L. Zhou, W. Fraunhofer, Impact of short range hydrophobic interactions and long range electrostatic forces on the aggregation kinetics of a monoclonal antibody and a dual-variable domain immunoglobulin at low and high concentrations, Int. J. Pharm. 421 (2011) 82-93.
    • (2011) Int. J. Pharm. , vol.421 , pp. 82-93
    • Kumar, V.1    Dixit, N.2    Zhou, L.L.3    Fraunhofer, W.4
  • 20
    • 84921055709 scopus 로고    scopus 로고
    • Dual-mode characterization of particulates
    • patent
    • E. N. Lewis, Malvern Instruments, Dual-mode characterization of particulates, patent WO/2013/027034 (2013).
    • (2013)
    • Lewis, E.N.1    Instruments, M.2
  • 21
    • 0033966565 scopus 로고    scopus 로고
    • Erratum [Molten globule-like state of human serum albumin at low pH, 266, pp. 26-34, 1999]
    • S. Muzammil, Y. Kumar, S. Tayyab, Erratum [Molten globule-like state of human serum albumin at low pH, 266, pp. 26-34, 1999], Eur. J. Biochem. 267 (2000) 1261.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1261
    • Muzammil, S.1    Kumar, Y.2    Tayyab, S.3
  • 22
    • 33644533167 scopus 로고    scopus 로고
    • The effect of solvent environment on the conformation and stability of human polyclonal IgG in solution
    • A. Szenczi, J. Kardos, G.A. Medgyesi, P. Zavodszky, The effect of solvent environment on the conformation and stability of human polyclonal IgG in solution, Biologicals 34 (2006) 5-14.
    • (2006) Biologicals , vol.34 , pp. 5-14
    • Szenczi, A.1    Kardos, J.2    Medgyesi, G.A.3    Zavodszky, P.4
  • 23
    • 47749085443 scopus 로고    scopus 로고
    • Detection of conformational changes in immunoglobulin G using isothermal titration calorimetry with low-molecular-weight probes
    • T. Rispens, C.M. Lakemond, N.I. Derksen, R.C. Aalberse, Detection of conformational changes in immunoglobulin G using isothermal titration calorimetry with low-molecular-weight probes, Anal. Biochem. 380 (2008) 303-309.
    • (2008) Anal. Biochem. , vol.380 , pp. 303-309
    • Rispens, T.1    Lakemond, C.M.2    Derksen, N.I.3    Aalberse, R.C.4
  • 24
    • 49149131689 scopus 로고    scopus 로고
    • Reductive unfolding of serum albumins uncovered by Raman spectroscopy
    • C. David, S. Foley, C. Mavon, M. Enescu, Reductive unfolding of serum albumins uncovered by Raman spectroscopy, Biopolymers 89 (2008) 623-634.
    • (2008) Biopolymers , vol.89 , pp. 623-634
    • David, C.1    Foley, S.2    Mavon, C.3    Enescu, M.4
  • 26
    • 77957365471 scopus 로고    scopus 로고
    • Structural changes of human serum albumin in response to a low concentration of heavy ions
    • A. Saha, V.V. Yakovlev, Structural changes of human serum albumin in response to a low concentration of heavy ions, J. Biophotonics 3 (2010) 670-677.
    • (2010) J. Biophotonics , vol.3 , pp. 670-677
    • Saha, A.1    Yakovlev, V.V.2
  • 27
    • 84866290004 scopus 로고    scopus 로고
    • In situ monitoring of proteins during lyophilization using micro-Raman spectroscopy: A description of structural changes induced by dehydration
    • A. Hedoux, L. Paccou, S. Achir, Y. Guinet, In situ monitoring of proteins during lyophilization using micro-Raman spectroscopy: a description of structural changes induced by dehydration, J. Pharm. Sci. 101 (2012) 2316-2326.
    • (2012) J. Pharm. Sci. , vol.101 , pp. 2316-2326
    • Hedoux, A.1    Paccou, L.2    Achir, S.3    Guinet, Y.4
  • 29
    • 0344004860 scopus 로고    scopus 로고
    • A holistic approach to protein secondary structure characterization using amide I band Raman spectroscopy
    • S.U. Sane, S.M. Cramer, T.M. Przybycien, A holistic approach to protein secondary structure characterization using amide I band Raman spectroscopy, Anal. Biochem. 269 (1999) 255-272.
    • (1999) Anal. Biochem. , vol.269 , pp. 255-272
    • Sane, S.U.1    Cramer, S.M.2    Przybycien, T.M.3
  • 30
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • X.M. He, D.C. Carter, Atomic structure and chemistry of human serum albumin, Nature 358 (1992) 209-215.
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 31
    • 57949110254 scopus 로고    scopus 로고
    • Human serum albumin unfolding: A small-angle X-ray scattering and light scattering study
    • L. Galantini, C. Leggio, N.V. Pavel, Human serum albumin unfolding: a small-angle X-ray scattering and light scattering study, J. Phys. Chem. B 112 (2008) 15460-15469.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 15460-15469
    • Galantini, L.1    Leggio, C.2    Pavel, N.V.3
  • 33
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
    • M. Bouchard, J. Zurdo, E.J. Nettleton, C.M. Dobson, C.V. Robinson, Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy, Protein Sci. 9 (2000) 1960-1967.
    • (2000) Protein Sci. , vol.9 , pp. 1960-1967
    • Bouchard, M.1    Zurdo, J.2    Nettleton, E.J.3    Dobson, C.M.4    Robinson, C.V.5
  • 34
    • 12844274977 scopus 로고    scopus 로고
    • Secondary Structure, Conformational Stability, and Glycosylation of a Recombinant Candida Rugosa Lipase Studied by Fourier-transform Infrared Spectroscopy
    • A. Natalello, D. Ami, S. Brocca, M. Lotti, S.M. Doglia, Secondary structure, conformational stability, and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy, Biochem. J. 385 (2005) 511-517.
    • (2005) Biochem. J. , vol.385 , pp. 511-517
    • Natalello, A.1    Ami, D.2    Brocca, S.3    Lotti, M.4    Doglia, S.M.5
  • 35
    • 3042771787 scopus 로고    scopus 로고
    • Structural stability and dynamics of hydrogenated and perdeuterated cytochrome P450cam (CYP101)
    • F. Meilleur, J. Contzen, D.A. Myles, C. Jung, Structural stability and dynamics of hydrogenated and perdeuterated cytochrome P450cam (CYP101), Biochemistry 43 (2004) 8744-8753.
    • (2004) Biochemistry , vol.43 , pp. 8744-8753
    • Meilleur, F.1    Contzen, J.2    Myles, D.A.3    Jung, C.4
  • 36
    • 0015935434 scopus 로고
    • Reversible denaturation of human serum albumin by pH, temperature, and guanidine hydrochloride followed by optical rotation
    • K. Wallevik, Reversible denaturation of human serum albumin by pH, temperature, and guanidine hydrochloride followed by optical rotation, J. Biol. Chem. 248 (1973) 2650-2655.
    • (1973) J. Biol. Chem. , vol.248 , pp. 2650-2655
    • Wallevik, K.1
  • 37
    • 0030976566 scopus 로고    scopus 로고
    • Thermodynamic features of the thermal unfolding of human serum albumin
    • G.A. Pico, Thermodynamic features of the thermal unfolding of human serum albumin, Int. J. Biol. Macromol. 20 (1997) 63-73.
    • (1997) Int. J. Biol. Macromol. , vol.20 , pp. 63-73
    • Pico, G.A.1
  • 38
    • 0032751222 scopus 로고    scopus 로고
    • Thermodynamic features of the chemical and thermal denaturations of human serum albumin
    • B. Farruggia, G.A. Pico, Thermodynamic features of the chemical and thermal denaturations of human serum albumin, Int. J. Biol. Macromol. 26 (1999) 317-323.
    • (1999) Int. J. Biol. Macromol. , vol.26 , pp. 317-323
    • Farruggia, B.1    Pico, G.A.2
  • 39
    • 0031852954 scopus 로고    scopus 로고
    • Unfolding of acrylodan-labeled human serum albumin probed by steady-state and time-resolved fluorescence methods
    • K. Flora, J.D. Brennan, G.A. Baker, M.A. Doody, F.V. Bright, Unfolding of acrylodan-labeled human serum albumin probed by steady-state and time-resolved fluorescence methods, Biophys. J. 75 (1998) 1084-1096.
    • (1998) Biophys. J. , vol.75 , pp. 1084-1096
    • Flora, K.1    Brennan, J.D.2    Baker, G.A.3    Doody, M.A.4    Bright, F.V.5
  • 40
    • 38349019572 scopus 로고    scopus 로고
    • Spectroscopic studies on the effect of temperature on pH-induced folded states of human serum albumin
    • A.K. Shaw, S.K. Pal, Spectroscopic studies on the effect of temperature on pH-induced folded states of human serum albumin, J. Photochem. Photobiol., B 90 (2008) 69-77.
    • (2008) J. Photochem. Photobiol., B , vol.90 , pp. 69-77
    • Shaw, A.K.1    Pal, S.K.2
  • 41
    • 84895502551 scopus 로고    scopus 로고
    • Oxidation of therapeutic proteins and peptides: Structural and biological consequences
    • R. Torosantucci, C. Schoneich, W. Jiskoot, Oxidation of therapeutic proteins and peptides: structural and biological consequences, Pharm. Res. 31 (2014) 541-553.
    • (2014) Pharm. Res. , vol.31 , pp. 541-553
    • Torosantucci, R.1    Schoneich, C.2    Jiskoot, W.3
  • 44
    • 77950236865 scopus 로고    scopus 로고
    • Conformational changes in oxidatively stressed monoclonal antibodies studied by hydrogen exchange mass spectrometry
    • W. Burkitt, P. Domann, G. O'Connor, Conformational changes in oxidatively stressed monoclonal antibodies studied by hydrogen exchange mass spectrometry, Protein Sci. 19 (2010) 826-835.
    • (2010) Protein Sci. , vol.19 , pp. 826-835
    • Burkitt, W.1    Domann, P.2    O'Connor, G.3
  • 45
    • 77955412238 scopus 로고    scopus 로고
    • Post-translational modifications differentially affect IgG1 conformation and receptor binding
    • D. Houde, Y. Peng, S.A. Berkowitz, J.R. Engen, Post-translational modifications differentially affect IgG1 conformation and receptor binding, Mol. Cell. Proteomics 9 (2010) 1716-1728.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1716-1728
    • Houde, D.1    Peng, Y.2    Berkowitz, S.A.3    Engen, J.R.4
  • 46
    • 84883000780 scopus 로고    scopus 로고
    • Influence of methionine oxidation on the aggregation of recombinant human growth hormone
    • F. Mulinacci, E. Poirier, M.A. Capelle, R. Gurny, T. Arvinte, Influence of methionine oxidation on the aggregation of recombinant human growth hormone, Eur. J. Pharm. Biopharm. 85 (2013) 42-52.
    • (2013) Eur. J. Pharm. Biopharm. , vol.85 , pp. 42-52
    • Mulinacci, F.1    Poirier, E.2    Capelle, M.A.3    Gurny, R.4    Arvinte, T.5
  • 47
    • 84897130151 scopus 로고    scopus 로고
    • Oxidation enhances human serum albumin thermal stability and changes the routes of amyloid fibril formation
    • G. Sancataldo, V. Vetri, V. Fodera, G. Di Cara, V. Militello, M. Leone, Oxidation enhances human serum albumin thermal stability and changes the routes of amyloid fibril formation, PLoS ONE 9 (2014) e84552.
    • (2014) PLoS ONE , vol.9 , pp. e84552
    • Sancataldo, G.1    Vetri, V.2    Fodera, V.3    Di Cara, G.4    Militello, V.5    Leone, M.6
  • 50
    • 80052606544 scopus 로고    scopus 로고
    • Combined Raman and IR spectroscopic study on the radical-based modifications of methionine
    • A. Torreggiani, S. Barata-Vallejo, C. Chatgilialoglu, Combined Raman and IR spectroscopic study on the radical-based modifications of methionine, Anal. Bioanal. Chem. 401 (2011) 1231-1239.
    • (2011) Anal. Bioanal. Chem. , vol.401 , pp. 1231-1239
    • Torreggiani, A.1    Barata-Vallejo, S.2    Chatgilialoglu, C.3
  • 51
    • 84903372523 scopus 로고    scopus 로고
    • Developments and challenges for mAb-based therapeutics
    • S. Goswami, W. Wang, T. Arakawa, S. Ohtake, Developments and challenges for mAb-based therapeutics, Antibodies 2 (2013) 452-500.
    • (2013) Antibodies , vol.2 , pp. 452-500
    • Goswami, S.1    Wang, W.2    Arakawa, T.3    Ohtake, S.4
  • 53
    • 33947544337 scopus 로고    scopus 로고
    • Highly concentrated monoclonal antibody solutions: Direct analysis of physical structure and thermal stability
    • N. Harn, C. Allan, C. Oliver, C.R. Middaugh, Highly concentrated monoclonal antibody solutions: direct analysis of physical structure and thermal stability, J. Pharm. Sci. 96 (2007) 532-546.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 532-546
    • Harn, N.1    Allan, C.2    Oliver, C.3    Middaugh, C.R.4
  • 56
    • 17644421429 scopus 로고    scopus 로고
    • Dynamic light scattering application to study protein interactions in electrolyte solutions
    • S. Li, D. Xing, J. Li, Dynamic light scattering application to study protein interactions in electrolyte solutions, J. Biol. Phys. 30 (2004) 313-324.
    • (2004) J. Biol. Phys. , vol.30 , pp. 313-324
    • Li, S.1    Xing, D.2    Li, J.3
  • 58
    • 84855891967 scopus 로고    scopus 로고
    • Viscosity behavior of high-concentration monoclonal antibody solutions: Correlation with interaction parameter and electroviscous effects
    • S. Yadav, S.J. Shire, D.S. Kalonia, Viscosity behavior of high-concentration monoclonal antibody solutions: correlation with interaction parameter and electroviscous effects, J. Pharm. Sci. 101 (2012) 998-1011.
    • (2012) J. Pharm. Sci. , vol.101 , pp. 998-1011
    • Yadav, S.1    Shire, S.J.2    Kalonia, D.S.3
  • 59
    • 76649099495 scopus 로고    scopus 로고
    • Specific interactions in high concentration antibody solutions resulting in high viscosity
    • S. Yadav, J. Liu, S.J. Shire, D.S. Kalonia, Specific interactions in high concentration antibody solutions resulting in high viscosity, J. Pharm. Sci. 99 (2010) 1152-1168.
    • (2010) J. Pharm. Sci. , vol.99 , pp. 1152-1168
    • Yadav, S.1    Liu, J.2    Shire, S.J.3    Kalonia, D.S.4
  • 60
    • 81055133744 scopus 로고    scopus 로고
    • Thermal unfolding curves of high concentration bovine IgG measured by FTIR spectroscopy
    • V. Sathya Devi, D.R. Coleman, J. Truntzer, Thermal unfolding curves of high concentration bovine IgG measured by FTIR spectroscopy, Protein J. 30 (2011) 395-403.
    • (2011) Protein J. , vol.30 , pp. 395-403
    • Sathya Devi, V.1    Coleman, D.R.2    Truntzer, J.3
  • 61
    • 84876912537 scopus 로고    scopus 로고
    • Monitoring protein aggregation kinetics with simultaneous multiple sample light scattering
    • M.F. Drenski, M.L. Brader, R.W. Alston, W.F. Reed, Monitoring protein aggregation kinetics with simultaneous multiple sample light scattering, Anal. Biochem. 437 (2013) 185-197.
    • (2013) Anal. Biochem. , vol.437 , pp. 185-197
    • Drenski, M.F.1    Brader, M.L.2    Alston, R.W.3    Reed, W.F.4


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