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Volumn 63, Issue 13, 2011, Pages 1107-1117

Viscosity of concentrated therapeutic protein compositions

Author keywords

Antibody; Formulation; Rheology; Shear; Surfactant

Indexed keywords

ANTIBODIES; CHEMICAL STABILITY; ELASTICITY; MONOCLONAL ANTIBODIES; RHEOLOGY; SHEARING; SURFACE ACTIVE AGENTS; VISCOSITY;

EID: 80054726708     PISSN: 0169409X     EISSN: 18728294     Source Type: Journal    
DOI: 10.1016/j.addr.2011.09.008     Document Type: Review
Times cited : (123)

References (97)
  • 1
    • 2642550862 scopus 로고    scopus 로고
    • Challenges in the development of high protein concentration formulations
    • Shire S.J., Shahrokh Z., Liu J. Challenges in the development of high protein concentration formulations. J. Pharm. Sci. 2004, 93(6):1390-1402.
    • (2004) J. Pharm. Sci. , vol.93 , Issue.6 , pp. 1390-1402
    • Shire, S.J.1    Shahrokh, Z.2    Liu, J.3
  • 3
    • 27644477360 scopus 로고    scopus 로고
    • Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution
    • Liu J., Nguyen M.D., Andya J.D., Shire S.J. Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution. J. Pharm. Sci. 2005, 94(9):1928-1940.
    • (2005) J. Pharm. Sci. , vol.94 , Issue.9 , pp. 1928-1940
    • Liu, J.1    Nguyen, M.D.2    Andya, J.D.3    Shire, S.J.4
  • 4
  • 5
    • 0036265948 scopus 로고    scopus 로고
    • The role of intravenous immunoglobulin therapy in autoimmune and inflammatory disorders
    • Chiarini F., Emmi L. The role of intravenous immunoglobulin therapy in autoimmune and inflammatory disorders. Neurol. Sci. 2002, 23:S1-S8.
    • (2002) Neurol. Sci. , vol.23
    • Chiarini, F.1    Emmi, L.2
  • 6
  • 7
    • 0025843479 scopus 로고
    • A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme
    • Goldberg M.E., Rudolph R., Jaenicke R. A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme. Biochemistry 1991, 30(11):2790-2797.
    • (1991) Biochemistry , vol.30 , Issue.11 , pp. 2790-2797
    • Goldberg, M.E.1    Rudolph, R.2    Jaenicke, R.3
  • 8
    • 0037117499 scopus 로고    scopus 로고
    • Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparraguine-rich domains of Su35 and of the amyloid beta-peptide of amyloid plaques
    • Perutz M.F., Pope B.J., Owen D., Wanker E.E., Scherzinger E. Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparraguine-rich domains of Su35 and of the amyloid beta-peptide of amyloid plaques. Proc. Natl. Acad. Sci. U. S. A. 2002, 99(8):5596-5600.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , Issue.8 , pp. 5596-5600
    • Perutz, M.F.1    Pope, B.J.2    Owen, D.3    Wanker, E.E.4    Scherzinger, E.5
  • 11
    • 0029947485 scopus 로고    scopus 로고
    • Stoichiometric and substoichiometric inhibition of tubulin self-assembly by colchicine analogs
    • Perez-Ramirez B., Andreu J.M., Gorbunoff M.J., Timasheff S.N. Stoichiometric and substoichiometric inhibition of tubulin self-assembly by colchicine analogs. Biochemistry 1996, 35(10):3277-3285.
    • (1996) Biochemistry , vol.35 , Issue.10 , pp. 3277-3285
    • Perez-Ramirez, B.1    Andreu, J.M.2    Gorbunoff, M.J.3    Timasheff, S.N.4
  • 12
    • 24344493485 scopus 로고    scopus 로고
    • Probing reversible self-association of therapeutic proteins by sedimentation velocity in the analytical ultracentrifuge
    • Perez-Ramirez B., Steckert J.J. Probing reversible self-association of therapeutic proteins by sedimentation velocity in the analytical ultracentrifuge. Methods Mol. Biol. 2005, 308:301-318.
    • (2005) Methods Mol. Biol. , vol.308 , pp. 301-318
    • Perez-Ramirez, B.1    Steckert, J.J.2
  • 14
    • 0001002352 scopus 로고
    • Conformation changes of proteins
    • Lumry R., Eyring H. Conformation changes of proteins. J. Phys. Chem. 1954, 58:110-120.
    • (1954) J. Phys. Chem. , vol.58 , pp. 110-120
    • Lumry, R.1    Eyring, H.2
  • 16
    • 0037421836 scopus 로고    scopus 로고
    • Kinetics of irreversible protein aggregation: analysis of extended Lumry-Eyring models and implications for predicting protein shelf life
    • Roberts C.J. Kinetics of irreversible protein aggregation: analysis of extended Lumry-Eyring models and implications for predicting protein shelf life. J. Phys. Chem. B 2003, 107(5):1194-1207.
    • (2003) J. Phys. Chem. B , vol.107 , Issue.5 , pp. 1194-1207
    • Roberts, C.J.1
  • 17
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: mechanism and driving forces in non-native protein aggregation
    • Chi E.Y., Krishnan S., Randolph T.W., Carpenter J.F. Physical stability of proteins in aqueous solution: mechanism and driving forces in non-native protein aggregation. Pharm. Res. 2003, 20(9):1325-1336.
    • (2003) Pharm. Res. , vol.20 , Issue.9 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 18
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated
    • Timasheff S.N. Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv. Prot. Chem. 1998, 51:355-432.
    • (1998) Adv. Prot. Chem. , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 19
    • 0019888281 scopus 로고
    • The stabilization of proteins by sucrose
    • Lee J.C., Timasheff S.N. The stabilization of proteins by sucrose. J. Biol. Chem. 1981, 256(14):7193-7201.
    • (1981) J. Biol. Chem. , vol.256 , Issue.14 , pp. 7193-7201
    • Lee, J.C.1    Timasheff, S.N.2
  • 20
    • 0020477017 scopus 로고
    • Stabilization of protein structure by sugars
    • Arakawa T., Timasheff S.N. Stabilization of protein structure by sugars. Biochemistry 1982, 21(25):6536-6544.
    • (1982) Biochemistry , vol.21 , Issue.25 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 21
    • 0030040794 scopus 로고    scopus 로고
    • On the role of surface tension in the stabilization of globular proteins
    • Lin T.Y., Timasheff S.N. On the role of surface tension in the stabilization of globular proteins. Protein Sci. 1996, 5(2):372-381.
    • (1996) Protein Sci. , vol.5 , Issue.2 , pp. 372-381
    • Lin, T.Y.1    Timasheff, S.N.2
  • 22
    • 32644484736 scopus 로고    scopus 로고
    • Effects of ultra-/diafiltration conditions on present aggregates in human IgG preparations
    • Ahrer K., Buchacher A., Iberer G., Jungbauer A. Effects of ultra-/diafiltration conditions on present aggregates in human IgG preparations. J. Membr. Sci. 2006, 274:108-115.
    • (2006) J. Membr. Sci. , vol.274 , pp. 108-115
    • Ahrer, K.1    Buchacher, A.2    Iberer, G.3    Jungbauer, A.4
  • 23
    • 34250728543 scopus 로고    scopus 로고
    • High concentration formulation feasibility of human immunoglubulin G for subcutaneous administration
    • Dani B., Platz R., Tzannis S.T. High concentration formulation feasibility of human immunoglubulin G for subcutaneous administration. J. Pharm. Sci. 2007, 96(6):1504-1517.
    • (2007) J. Pharm. Sci. , vol.96 , Issue.6 , pp. 1504-1517
    • Dani, B.1    Platz, R.2    Tzannis, S.T.3
  • 24
    • 70449704158 scopus 로고    scopus 로고
    • Formulation and manufacturability of biologics
    • Shire S.J. Formulation and manufacturability of biologics. Curr. Opin. Biotechnol. 2009, 20(6):708-714.
    • (2009) Curr. Opin. Biotechnol. , vol.20 , Issue.6 , pp. 708-714
    • Shire, S.J.1
  • 25
    • 44449108578 scopus 로고    scopus 로고
    • Nature and consequences of protein-protein interactions in high protein concentration solutions
    • Saluja A., Kalonia D.S. Nature and consequences of protein-protein interactions in high protein concentration solutions. Int. J. Pharm. 2008, 358(1-2):1-15.
    • (2008) Int. J. Pharm. , vol.358 , Issue.1-2 , pp. 1-15
    • Saluja, A.1    Kalonia, D.S.2
  • 26
    • 0003869338 scopus 로고
    • Chapman and Hall, London
    • Walters K. Rheometry 1975, Chapman and Hall, London.
    • (1975) Rheometry
    • Walters, K.1
  • 27
    • 3242659055 scopus 로고
    • Official nomenclature for material functions describing the response of a viscoelastic fluid to various shearing and extensional deformations
    • Dealy J.M. Official nomenclature for material functions describing the response of a viscoelastic fluid to various shearing and extensional deformations. J. Rheol. 1995, 39(1):253-265.
    • (1995) J. Rheol. , vol.39 , Issue.1 , pp. 253-265
    • Dealy, J.M.1
  • 34
    • 55749113694 scopus 로고    scopus 로고
    • Reversible self-association of a concentrated monoclonal antibody solution mediated by Fab-Fab interaction that impacts solution viscosity
    • Kanai S., Liu J., Patapoff T.W., Shire S.J. Reversible self-association of a concentrated monoclonal antibody solution mediated by Fab-Fab interaction that impacts solution viscosity. J. Pharm. Sci. 2008, 97:4219-4227.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 4219-4227
    • Kanai, S.1    Liu, J.2    Patapoff, T.W.3    Shire, S.J.4
  • 35
    • 80054749303 scopus 로고    scopus 로고
    • Review of converging flow methods for determining the extensional flow behaviour of polymer melts
    • Rides M., Chakravorty S. Review of converging flow methods for determining the extensional flow behaviour of polymer melts. NPL Report CMMT(A) 1997, 80.
    • (1997) NPL Report CMMT(A) , vol.80
    • Rides, M.1    Chakravorty, S.2
  • 36
    • 84987041184 scopus 로고
    • Converging flow of polymer melts in extrusion dies
    • Cogswell F.N. Converging flow of polymer melts in extrusion dies. Polym. Eng. Sci. 1972, 12(1):64-73.
    • (1972) Polym. Eng. Sci. , vol.12 , Issue.1 , pp. 64-73
    • Cogswell, F.N.1
  • 37
    • 0023979323 scopus 로고
    • An approximate analysis for contraction and converging flows
    • Binding D.M. An approximate analysis for contraction and converging flows. J. Non-Newton. Fluid Mech. 1988, 27:173-189.
    • (1988) J. Non-Newton. Fluid Mech. , vol.27 , pp. 173-189
    • Binding, D.M.1
  • 38
    • 0026392291 scopus 로고
    • Further considerations of axisymmetric contraction flows
    • Binding D.M. Further considerations of axisymmetric contraction flows. J. Non-Newton. Fluid Mech. 1991, 41:27-42.
    • (1991) J. Non-Newton. Fluid Mech. , vol.41 , pp. 27-42
    • Binding, D.M.1
  • 42
    • 0023952837 scopus 로고
    • Capillary viscometry study of non-Newtonian fluids: influence of viscous heating
    • Duda J.L., Klaus E.E., Lin S.C. Capillary viscometry study of non-Newtonian fluids: influence of viscous heating. Ind. Eng. Chem. Res. 1988, 27:352-361.
    • (1988) Ind. Eng. Chem. Res. , vol.27 , pp. 352-361
    • Duda, J.L.1    Klaus, E.E.2    Lin, S.C.3
  • 45
    • 0032899569 scopus 로고    scopus 로고
    • Does the viscosity of glycerin fall at high shear rates?
    • Dontula P., Macosko C.W., Scriven L.E. Does the viscosity of glycerin fall at high shear rates?. Ind. Eng. Chem. Res. 1999, 38:1729-1735.
    • (1999) Ind. Eng. Chem. Res. , vol.38 , pp. 1729-1735
    • Dontula, P.1    Macosko, C.W.2    Scriven, L.E.3
  • 46
    • 0022048024 scopus 로고
    • High shear viscometry with a rotation parallel-disk device
    • Connelly R.W., Greener J. High shear viscometry with a rotation parallel-disk device. J. Rheol. 1985, 29(2):209-226.
    • (1985) J. Rheol. , vol.29 , Issue.2 , pp. 209-226
    • Connelly, R.W.1    Greener, J.2
  • 48
    • 31144465928 scopus 로고    scopus 로고
    • On the gap error in parallel plate rheometry that arises from the presence of air when zeroing the gap
    • Davies G.A., Stokes J.R. On the gap error in parallel plate rheometry that arises from the presence of air when zeroing the gap. J. Rheol. 2005, 49(4):919-922.
    • (2005) J. Rheol. , vol.49 , Issue.4 , pp. 919-922
    • Davies, G.A.1    Stokes, J.R.2
  • 50
    • 0000156563 scopus 로고
    • Correlation of dynamic and steady flow viscosities
    • Cox W.P., Merz E.H. Correlation of dynamic and steady flow viscosities. J. Polymer Sci. 1958, 28:619-622.
    • (1958) J. Polymer Sci. , vol.28 , pp. 619-622
    • Cox, W.P.1    Merz, E.H.2
  • 51
    • 0010252237 scopus 로고
    • Correlation of dynamic and steady flow viscosities of filled polymer systems
    • Kitano T., Nishimura T., Kataoka T., Sakai T. Correlation of dynamic and steady flow viscosities of filled polymer systems. Rheologica Acta 1980, 19(5):671-673.
    • (1980) Rheologica Acta , vol.19 , Issue.5 , pp. 671-673
    • Kitano, T.1    Nishimura, T.2    Kataoka, T.3    Sakai, T.4
  • 52
    • 0019044222 scopus 로고
    • Dynamic and steady state rheological measurements on polymer melts
    • Shulken R.M., Cox R.H., Minnick L.A. Dynamic and steady state rheological measurements on polymer melts. J. Appl. Polym. Sci. 1980, 25:1341-1353.
    • (1980) J. Appl. Polym. Sci. , vol.25 , pp. 1341-1353
    • Shulken, R.M.1    Cox, R.H.2    Minnick, L.A.3
  • 53
    • 70449436442 scopus 로고    scopus 로고
    • Polysorbate 20 prevents the precipitation of a monoclonal antibody during shear
    • Patapoff T.W., Esue O. Polysorbate 20 prevents the precipitation of a monoclonal antibody during shear. Pharm. Dev. Technol. 2009, 14(6):659-664.
    • (2009) Pharm. Dev. Technol. , vol.14 , Issue.6 , pp. 659-664
    • Patapoff, T.W.1    Esue, O.2
  • 54
    • 17444372417 scopus 로고    scopus 로고
    • High shear microfluidics and its application in rheological measurement
    • Kang K., Lee L.J., Koelling K.W. High shear microfluidics and its application in rheological measurement. Exp. Fluids 2005, 38:222-232.
    • (2005) Exp. Fluids , vol.38 , pp. 222-232
    • Kang, K.1    Lee, L.J.2    Koelling, K.W.3
  • 55
    • 43849104776 scopus 로고    scopus 로고
    • Rheological behaviour of low/high density polyethylene melt flowing through micro-channels
    • Chen C.S. Rheological behaviour of low/high density polyethylene melt flowing through micro-channels. e-Polymers 2008, 039.
    • (2008) e-Polymers , vol.39
    • Chen, C.S.1
  • 56
    • 77649185864 scopus 로고    scopus 로고
    • High-throughput dynamic light scattering method for measuring viscosity of concentrated protein solutions
    • He F., Becker G.W., Litowski J.R., Narhi L.O., Brems D.N., Razinkov V.I. High-throughput dynamic light scattering method for measuring viscosity of concentrated protein solutions. Anal. Biochem. 2010, 399(1):141-143.
    • (2010) Anal. Biochem. , vol.399 , Issue.1 , pp. 141-143
    • He, F.1    Becker, G.W.2    Litowski, J.R.3    Narhi, L.O.4    Brems, D.N.5    Razinkov, V.I.6
  • 57
    • 69249213351 scopus 로고    scopus 로고
    • Lysozyme as diffusion tracer for measuring aqueous solution viscosity
    • Parmar A.S., Muschol M. Lysozyme as diffusion tracer for measuring aqueous solution viscosity. J. Colloid Interface Sci. 2009, 339(1):243-248.
    • (2009) J. Colloid Interface Sci. , vol.339 , Issue.1 , pp. 243-248
    • Parmar, A.S.1    Muschol, M.2
  • 59
    • 0017985434 scopus 로고
    • Viscosity of liquid water in the range -8°C to 150°C
    • Kestin J., Sokolov M., Wakeham W.A. Viscosity of liquid water in the range -8°C to 150°C. J. Phys. Chem. Ref. Data 1978, 7(3):941-948.
    • (1978) J. Phys. Chem. Ref. Data , vol.7 , Issue.3 , pp. 941-948
    • Kestin, J.1    Sokolov, M.2    Wakeham, W.A.3
  • 60
    • 0041931122 scopus 로고    scopus 로고
    • Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges
    • Hall D., Minton A.P. Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges. Biochim. Biophys. Acta 2003, 1649(2):127-139.
    • (2003) Biochim. Biophys. Acta , vol.1649 , Issue.2 , pp. 127-139
    • Hall, D.1    Minton, A.P.2
  • 61
    • 0020184671 scopus 로고
    • How crowded is the cytoplasm?
    • Fulton A.B. How crowded is the cytoplasm?. Cell 1982, 30:345-347.
    • (1982) Cell , vol.30 , pp. 345-347
    • Fulton, A.B.1
  • 62
    • 0027318513 scopus 로고
    • Macromolecular crowding: biochemical, biophysical, and physiological consequences
    • Zimmerman S.B., Minton A.P. Macromolecular crowding: biochemical, biophysical, and physiological consequences. Annu. Rev. Biophys. Biomol. Struct. 1993, 22:27-65.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 63
    • 0041822089 scopus 로고    scopus 로고
    • Cell biology: join the crowd
    • Ellis R.J., Minton A.P. Cell biology: join the crowd. Nature 2003, 425(6953):27-28.
    • (2003) Nature , vol.425 , Issue.6953 , pp. 27-28
    • Ellis, R.J.1    Minton, A.P.2
  • 64
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: preparing the next generation of molecular biologists
    • Alberts B. The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell 1998, 92(3):291-294.
    • (1998) Cell , vol.92 , Issue.3 , pp. 291-294
    • Alberts, B.1
  • 65
    • 70449112652 scopus 로고    scopus 로고
    • Long- and short-range electrostatic interactions affect the rheology of highly concentrated antibody solutions
    • Chari R., Jerath K., Badkar A., Kalonia D.S. Long- and short-range electrostatic interactions affect the rheology of highly concentrated antibody solutions. Pharm. Res. 2009, 26(12):2607-2618.
    • (2009) Pharm. Res. , vol.26 , Issue.12 , pp. 2607-2618
    • Chari, R.1    Jerath, K.2    Badkar, A.3    Kalonia, D.S.4
  • 66
    • 38149037129 scopus 로고    scopus 로고
    • Ultrasonic rheology of a monoclonal antibody (IgG2) solution: implications for physical stability of proteins in high concentration formulations
    • Saluja A., Badkar A., Zeng D.L., Kalonia D.S. Ultrasonic rheology of a monoclonal antibody (IgG2) solution: implications for physical stability of proteins in high concentration formulations. J. Pharm. Sci. 2007, 96(12):3181-3195.
    • (2007) J. Pharm. Sci. , vol.96 , Issue.12 , pp. 3181-3195
    • Saluja, A.1    Badkar, A.2    Zeng, D.L.3    Kalonia, D.S.4
  • 67
    • 0019764210 scopus 로고
    • Self-association in highly concentrated solutions of myoglobin: a novel analysis of sedimentation equilibrium of highly nonideal solutions
    • Minton A.P., Lewis M.S. Self-association in highly concentrated solutions of myoglobin: a novel analysis of sedimentation equilibrium of highly nonideal solutions. Biophys. Chem. 1981, 14(4):317-324.
    • (1981) Biophys. Chem. , vol.14 , Issue.4 , pp. 317-324
    • Minton, A.P.1    Lewis, M.S.2
  • 68
    • 0021690181 scopus 로고
    • Reversible self-association of a human myeloma protein. Thermodynamics and relevance to viscosity effects and solubility
    • Hall C.G., Abraham G.N. Reversible self-association of a human myeloma protein. Thermodynamics and relevance to viscosity effects and solubility. Biochemistry 1984, 23:5123-5129.
    • (1984) Biochemistry , vol.23 , pp. 5123-5129
    • Hall, C.G.1    Abraham, G.N.2
  • 69
    • 0021149471 scopus 로고
    • Size, shape, and hydration of a self associating human IgG myeloma protein: axial asymmetry as a contributing factor in serum hyperviscosity
    • Hall C.G., Abraham G.N. Size, shape, and hydration of a self associating human IgG myeloma protein: axial asymmetry as a contributing factor in serum hyperviscosity. Arch. Biochem. Biophys. 1984, 233(2):330-337.
    • (1984) Arch. Biochem. Biophys. , vol.233 , Issue.2 , pp. 330-337
    • Hall, C.G.1    Abraham, G.N.2
  • 70
    • 34547515360 scopus 로고    scopus 로고
    • Effect of solutes on the viscosity of supercritical solutions
    • Abbott A.P., Hope E.G., Palmer D.J. Effect of solutes on the viscosity of supercritical solutions. J. Phys. Chem. B 2007, 111:8114-8118.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 8114-8118
    • Abbott, A.P.1    Hope, E.G.2    Palmer, D.J.3
  • 71
    • 34447566117 scopus 로고    scopus 로고
    • Quantitative characterization of weak self-association in concentrated solutions of immunoglobulin G via the measurement of sedimentation equilibrium and osmotic pressure
    • Jimenez M., Rivas G., Minton A.P. Quantitative characterization of weak self-association in concentrated solutions of immunoglobulin G via the measurement of sedimentation equilibrium and osmotic pressure. Biochemistry 2007, 46(28):8373-8378.
    • (2007) Biochemistry , vol.46 , Issue.28 , pp. 8373-8378
    • Jimenez, M.1    Rivas, G.2    Minton, A.P.3
  • 72
    • 33845965334 scopus 로고    scopus 로고
    • Ultrasonic storage modulus as a novel parameter for analyzing protein-protein interactions in high protein concentration solutions: correlation with static and dynamic light scattering measurements
    • Saluja A., Badkar A.V., Zeng D.L., Nema S., Kalonia D.S. Ultrasonic storage modulus as a novel parameter for analyzing protein-protein interactions in high protein concentration solutions: correlation with static and dynamic light scattering measurements. Biophys. J. 2007, 92(1):234-244.
    • (2007) Biophys. J. , vol.92 , Issue.1 , pp. 234-244
    • Saluja, A.1    Badkar, A.V.2    Zeng, D.L.3    Nema, S.4    Kalonia, D.S.5
  • 73
    • 0032484699 scopus 로고    scopus 로고
    • Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes
    • Curtis R.A., Prausnitz J.M., Blanch H.W. Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes. Biotechnol. Bioeng. 1998, 57:11-21.
    • (1998) Biotechnol. Bioeng. , vol.57 , pp. 11-21
    • Curtis, R.A.1    Prausnitz, J.M.2    Blanch, H.W.3
  • 74
    • 0036468995 scopus 로고    scopus 로고
    • Kinetic studies of protein-protein interactions
    • Schreiber G. Kinetic studies of protein-protein interactions. Curr. Opin. Struct. Biol. 2002, 12:41-47.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 41-47
    • Schreiber, G.1
  • 75
    • 30044440719 scopus 로고    scopus 로고
    • Characterizing the aggregation and conformation of protein therapeutics
    • Philo J.S. Characterizing the aggregation and conformation of protein therapeutics. Am. Biotechnol. Lab. 2003, 21:22-26.
    • (2003) Am. Biotechnol. Lab. , vol.21 , pp. 22-26
    • Philo, J.S.1
  • 76
    • 0027410312 scopus 로고
    • Rapid and accurate microfractionation of the contents of small centrifuge tubes: application in the measurement of molecular weight of proteins via sedimentation equilibrium
    • Darawshe S., Rivas G., Minton A.P. Rapid and accurate microfractionation of the contents of small centrifuge tubes: application in the measurement of molecular weight of proteins via sedimentation equilibrium. Anal. Biochem. 1993, 209:130-135.
    • (1993) Anal. Biochem. , vol.209 , pp. 130-135
    • Darawshe, S.1    Rivas, G.2    Minton, A.P.3
  • 77
    • 0028284639 scopus 로고
    • Quantitative characterization of macromolecular associations in solution via real-time and postcentrifugation measurements of sedimentation equilibrium: a comparison
    • Darawshe S., Minton A.P. Quantitative characterization of macromolecular associations in solution via real-time and postcentrifugation measurements of sedimentation equilibrium: a comparison. Anal. Biochem. 1994, 220:1-4.
    • (1994) Anal. Biochem. , vol.220 , pp. 1-4
    • Darawshe, S.1    Minton, A.P.2
  • 78
    • 68949093728 scopus 로고    scopus 로고
    • Viscoelastic characterization of high concentration antibody formulations using quartz crystal microbalance with dissipation monitoring
    • Patel A.R., Kerwin B.A., Kanapuram S.R. Viscoelastic characterization of high concentration antibody formulations using quartz crystal microbalance with dissipation monitoring. J. Pharm. Sci. 2009, 98(9):3108-3116.
    • (2009) J. Pharm. Sci. , vol.98 , Issue.9 , pp. 3108-3116
    • Patel, A.R.1    Kerwin, B.A.2    Kanapuram, S.R.3
  • 79
    • 33748937041 scopus 로고    scopus 로고
    • Application of high-frequency rheology measurements for analyzing protein-protein interactions in high protein concentration solutions using a model monoclonal antibody (IgG2)
    • Saluja A., Badkar A.V., Zeng D.L., Nema S., Kalonia D.S. Application of high-frequency rheology measurements for analyzing protein-protein interactions in high protein concentration solutions using a model monoclonal antibody (IgG2). J. Pharm. Sci. 2006, 95:1967-1983.
    • (2006) J. Pharm. Sci. , vol.95 , pp. 1967-1983
    • Saluja, A.1    Badkar, A.V.2    Zeng, D.L.3    Nema, S.4    Kalonia, D.S.5
  • 80
    • 5344261276 scopus 로고
    • The application of the Bjerrum ion association theory to the binding of anions by proteins
    • Schellman J.A. The application of the Bjerrum ion association theory to the binding of anions by proteins. J. Phys. Chem. 1953, 57(4):472-475.
    • (1953) J. Phys. Chem. , vol.57 , Issue.4 , pp. 472-475
    • Schellman, J.A.1
  • 81
    • 76649099495 scopus 로고    scopus 로고
    • Specific interactions in high concentration antibody solutions resulting in high viscosity
    • Yadav S., Liu J., Shire S.J., Kalonia D.S. Specific interactions in high concentration antibody solutions resulting in high viscosity. J. Pharm. Sci. 2010, 99(3):1152-1168.
    • (2010) J. Pharm. Sci. , vol.99 , Issue.3 , pp. 1152-1168
    • Yadav, S.1    Liu, J.2    Shire, S.J.3    Kalonia, D.S.4
  • 82
    • 0020764850 scopus 로고
    • The primary electroviscous effect
    • McDonogh R.W., Hunter R.J. The primary electroviscous effect. J. Rheol. 1983, 27:189-199.
    • (1983) J. Rheol. , vol.27 , pp. 189-199
    • McDonogh, R.W.1    Hunter, R.J.2
  • 83
    • 0017867824 scopus 로고
    • Rheology of suspensions of charged rigid spheres
    • Russel W.B. Rheology of suspensions of charged rigid spheres. J. Fluid Mech. 1978, 85:209-232.
    • (1978) J. Fluid Mech. , vol.85 , pp. 209-232
    • Russel, W.B.1
  • 84
    • 11744320872 scopus 로고
    • The viscosity of aqueous solutions of bovine serum albumin between pH 4.3 and 10.5
    • Tanford C., Buzzell J.G. The viscosity of aqueous solutions of bovine serum albumin between pH 4.3 and 10.5. J. Phys. Chem. 1956, 60:225-231.
    • (1956) J. Phys. Chem. , vol.60 , pp. 225-231
    • Tanford, C.1    Buzzell, J.G.2
  • 85
    • 0000681244 scopus 로고
    • The effect of charge and ionic strength on the viscosity of ribonuclease
    • Buzzell G.J., Tanford C. The effect of charge and ionic strength on the viscosity of ribonuclease. J. Phys. Chem. 1956, 60:1204-1207.
    • (1956) J. Phys. Chem. , vol.60 , pp. 1204-1207
    • Buzzell, G.J.1    Tanford, C.2
  • 86
    • 21344457192 scopus 로고    scopus 로고
    • Application of ultrasonic shear rheometer to characterize rheological properties of high protein concentration solutions at microliter volume
    • Saluja A., Kalonia D.S. Application of ultrasonic shear rheometer to characterize rheological properties of high protein concentration solutions at microliter volume. J. Pharm. Sci. 2005, 94:1161-1168.
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1161-1168
    • Saluja, A.1    Kalonia, D.S.2
  • 87
    • 0035142983 scopus 로고    scopus 로고
    • Calculation of weak protein-protein interactions: the pH dependence of the second virial coefficient
    • Elcock A.H., McCammon J.A. Calculation of weak protein-protein interactions: the pH dependence of the second virial coefficient. Biophys. J. 2001, 80:613-625.
    • (2001) Biophys. J. , vol.80 , pp. 613-625
    • Elcock, A.H.1    McCammon, J.A.2
  • 88
    • 66349132473 scopus 로고    scopus 로고
    • Increasing IgG concentration modulates the conformational heterogeneity and bonding network that influence solution properties
    • Kamerzell T.J., Kanai S., Liu J., Shire S.J., Wang Y.J. Increasing IgG concentration modulates the conformational heterogeneity and bonding network that influence solution properties. J. Phys. Chem. B. 2009, 113(17):6109-6118.
    • (2009) J. Phys. Chem. B. , vol.113 , Issue.17 , pp. 6109-6118
    • Kamerzell, T.J.1    Kanai, S.2    Liu, J.3    Shire, S.J.4    Wang, Y.J.5
  • 89
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • Barth A., Zscherp C. What vibrations tell us about proteins. Q. Rev. Biophys. 2002, 35(4):369-430.
    • (2002) Q. Rev. Biophys. , vol.35 , Issue.4 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 90
    • 0029002812 scopus 로고
    • The conformational analysis of peptides using Fourier transform IR spectroscopy
    • Haris P.I., Chapman D. The conformational analysis of peptides using Fourier transform IR spectroscopy. Biopolymers 1995, 37(4):251-263.
    • (1995) Biopolymers , vol.37 , Issue.4 , pp. 251-263
    • Haris, P.I.1    Chapman, D.2
  • 91
    • 0035887070 scopus 로고    scopus 로고
    • Fourier transform infrared spectrometric analysis of protein conformation: effect of sampling method and stress factors
    • van de Weert M., Haris P.I., Hennink W.E., Crommelin D.J. Fourier transform infrared spectrometric analysis of protein conformation: effect of sampling method and stress factors. Anal. Biochem. 2001, 297(2):160-169.
    • (2001) Anal. Biochem. , vol.297 , Issue.2 , pp. 160-169
    • van de Weert, M.1    Haris, P.I.2    Hennink, W.E.3    Crommelin, D.J.4
  • 92
    • 80054769044 scopus 로고
    • Donnan equilibrium and the physical properties of proteins III. Viscosity
    • Loeb J.J. Donnan equilibrium and the physical properties of proteins III. Viscosity. Gen. Physiol. 1921, 827-841.
    • (1921) Gen. Physiol. , pp. 827-841
    • Loeb, J.J.1
  • 93
    • 84933846286 scopus 로고
    • Ion series and the physical properties of proteins. III. The action of salts in low concentration
    • Loeb J.J. Ion series and the physical properties of proteins. III. The action of salts in low concentration. Gen. Physiol. 1921, 391-414.
    • (1921) Gen. Physiol. , pp. 391-414
    • Loeb, J.J.1
  • 94
    • 80054762197 scopus 로고
    • The denaturation of antibody IV. The influence of pH and certain other factors on the rate of inactivation of Staphylococcus antitoxin in urea solutions
    • Wright G., Schomaker V. The denaturation of antibody IV. The influence of pH and certain other factors on the rate of inactivation of Staphylococcus antitoxin in urea solutions. J. Biol. Chem. 1948, 175(1):169-177.
    • (1948) J. Biol. Chem. , vol.175 , Issue.1 , pp. 169-177
    • Wright, G.1    Schomaker, V.2
  • 95
    • 85008191781 scopus 로고
    • Effect of physical and chemical factors on rheological behavior of commercial soy protein isolates: protein concentration, water imbibing capacity, salt addition, and thermal treatment
    • Wagner J.R., Sorgentini D.A., Anon M.C. Effect of physical and chemical factors on rheological behavior of commercial soy protein isolates: protein concentration, water imbibing capacity, salt addition, and thermal treatment. J. Agric. Food Chem. 1992, 40(10):1930-1937.
    • (1992) J. Agric. Food Chem. , vol.40 , Issue.10 , pp. 1930-1937
    • Wagner, J.R.1    Sorgentini, D.A.2    Anon, M.C.3
  • 96
    • 0030727624 scopus 로고    scopus 로고
    • The Hofmeister series: salt and solvent effects on interfacial phenomena
    • Cacace M.G., Landau E.M., Ramsden J.J. The Hofmeister series: salt and solvent effects on interfacial phenomena. Q. Rev. Biophys. 1997, 30(3):241-277.
    • (1997) Q. Rev. Biophys. , vol.30 , Issue.3 , pp. 241-277
    • Cacace, M.G.1    Landau, E.M.2    Ramsden, J.J.3
  • 97


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