메뉴 건너뛰기




Volumn 28, Issue 7, 2011, Pages 1750-1764

Establishing a link between amino acid sequences and self-associating and viscoelastic behavior of two closely related monoclonal antibodies

Author keywords

high concentration protein solution; intermolecular interactions; protein viscosity rheology; self association

Indexed keywords

MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 1; MONOCLONAL ANTIBODY 2; UNCLASSIFIED DRUG;

EID: 79959871746     PISSN: 07248741     EISSN: 1573904X     Source Type: Journal    
DOI: 10.1007/s11095-011-0410-0     Document Type: Article
Times cited : (110)

References (52)
  • 2
    • 79955877697 scopus 로고    scopus 로고
    • Challenges in the development of high protein concentration formulation
    • S.J. Shire W.R. Gombotz K.B. Peters J.D. Andya (eds). Springer New York. 10.1007/978-0-387-76643-0-9
    • Shire SJ, Zahra S, Liu J. Challenges in the development of high protein concentration formulation. In: Shire SJ, Gombotz WR, Peters KB, Andya JD, editors. Current trends in monoclonal antibody development and manufacturing. New York: Springer; 2010. p. 131-40.
    • (2010) Current Trends in Monoclonal Antibody Development and Manufacturing , pp. 131-40
    • Shire, S.J.1    Zahra, S.2    Liu, J.3
  • 3
    • 27644477360 scopus 로고    scopus 로고
    • Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution
    • DOI 10.1002/jps.20347
    • J Liu MDH Nguyen JD Andya SJ Shire 2005 Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution J Pharm Sci. 94 1928 40 16052543 10.1002/jps.20347 1:CAS:528: DC%2BD2MXpslOgt7g%3D (Pubitemid 41551477)
    • (2005) Journal of Pharmaceutical Sciences , vol.94 , Issue.9 , pp. 1928-1940
    • Liu, J.1    Nguyen, M.D.H.2    Andya, J.D.3    Shire, S.J.4
  • 4
    • 73949139940 scopus 로고    scopus 로고
    • Understanding and modulating opalescence and viscosity in a monoclonal antibody formulation
    • 10.1002/jps.21797
    • BA Salinas HA Sathish SM Bishop N Harn JF Carpenter TW Randolph 2009 Understanding and modulating opalescence and viscosity in a monoclonal antibody formulation J Pharm Sci. 99 82 93 10.1002/jps.21797
    • (2009) J Pharm Sci. , vol.99 , pp. 82-93
    • Salinas, B.A.1    Sathish, H.A.2    Bishop, S.M.3    Harn, N.4    Carpenter, J.F.5    Randolph, T.W.6
  • 6
    • 78049509357 scopus 로고    scopus 로고
    • Factors affecting the viscosity in high concentration solutions of different monoclonal antibodies
    • 20821382 10.1002/jps.22190 1:CAS:528:DC%2BC3cXhtlKjsbbI
    • S Yadav SJ Shire DS Kalonia 2010 Factors affecting the viscosity in high concentration solutions of different monoclonal antibodies J Pharm Sci. 99 4812 29 20821382 10.1002/jps.22190 1:CAS:528:DC%2BC3cXhtlKjsbbI
    • (2010) J Pharm Sci. , vol.99 , pp. 4812-29
    • Yadav, S.1    Shire, S.J.2    Kalonia, D.S.3
  • 7
    • 79959902221 scopus 로고    scopus 로고
    • Formulation and delivery issues for monoclonal antibody therapeutics
    • S.J. Shire W.R. Gombotz K.B. Peters J.D. Andya (eds). Springer New York. 10.1007/978-0-387-76643-0-8
    • Daugherty AL, Mrsny RJ. Formulation and delivery issues for monoclonal antibody therapeutics. In: Shire SJ, Gombotz WR, Peters KB, Andya JD, editors. Current trends in monoclonal antibody development and manufacturing. New York: Springer; 2010. p. 103-30.
    • (2010) Current Trends in Monoclonal Antibody Development and Manufacturing , pp. 103-30
    • Daugherty, A.L.1    Mrsny, R.J.2
  • 8
    • 0033969150 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for protein assembly
    • DOI 10.1016/S0959-440X(99)00045-7
    • AP Minton 2000 Implications of macromolecular crowding for protein assembly Curr Opin Struct Biol. 10 34 9 10679465 10.1016/S0959-440X(99)00045-7 1:CAS:528:DC%2BD3cXhs1Sltrs%3D (Pubitemid 30099324)
    • (2000) Current Opinion in Structural Biology , vol.10 , Issue.1 , pp. 34-39
    • Minton, A.P.1
  • 9
    • 25444487734 scopus 로고    scopus 로고
    • Influence of macromolecular crowding upon the stability and state of association of proteins: Predictions and observations
    • DOI 10.1002/jps.20417
    • AP Minton 2005 Influence of macromolecular crowding upon the stability and state of association of proteins: predictions and observations J Pharm Sci. 94 1668 75 15986476 10.1002/jps.20417 1:CAS:528:DC%2BD2MXnvVWnurY%3D (Pubitemid 41360861)
    • (2005) Journal of Pharmaceutical Sciences , vol.94 , Issue.8 , pp. 1668-1675
    • Minton, A.P.1
  • 10
    • 38149037129 scopus 로고    scopus 로고
    • 2) solution: Implications for physical stability of proteins in high concentration formulations
    • 17588261 10.1002/jps.20970 1:CAS:528:DC%2BD2sXhsVers7jE
    • 2) solution: implications for physical stability of proteins in high concentration formulations J Pharm Sci. 96 3181 95 17588261 10.1002/jps.20970 1:CAS:528:DC%2BD2sXhsVers7jE
    • (2007) J Pharm Sci. , vol.96 , pp. 3181-95
    • Saluja, A.1    Badkar, A.V.2    Zeng, D.L.3    Kalonia, D.S.4
  • 11
    • 55449104956 scopus 로고    scopus 로고
    • Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations
    • JD Andya CC Hsu SJ Shire 2003 Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations Pharm Sci. 5 E10
    • (2003) Pharm Sci. , vol.5 , pp. 10
    • Andya, J.D.1    Hsu, C.C.2    Shire, S.J.3
  • 12
    • 84989674897 scopus 로고
    • The photophysics and photochemistry of the near-UV absorbing amino acids. II. Tyrosine and its simple derivatives
    • 10.1111/j.1751-1097.1984.tb03891.x 1:CAS:528:DyaL2cXktVejtL4%3D
    • D Creed 1984 The photophysics and photochemistry of the near-UV absorbing amino acids. II. Tyrosine and its simple derivatives Photochem Photobiol. 39 563 75 10.1111/j.1751-1097.1984.tb03891.x 1:CAS:528:DyaL2cXktVejtL4%3D
    • (1984) Photochem Photobiol. , vol.39 , pp. 563-75
    • Creed, D.1
  • 13
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • DOI 10.1023/A:1025771421906
    • EY Chi S Krishnan TW Randolph JF Carpenter 2003 Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation Pharm Res. 20 1325 36 14567625 10.1023/A:1025771421906 1:CAS:528:DC%2BD3sXnt1KitLY%3D (Pubitemid 37164039)
    • (2003) Pharmaceutical Research , vol.20 , Issue.9 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 14
    • 27944485230 scopus 로고    scopus 로고
    • What factor drives the fibrillogenic association of β-sheets?
    • DOI 10.1016/j.febslet.2005.10.058, PII S0014579305013311
    • A Fernandez 2005 What factor drives the fibrillogenic association of β-sheets? FEBS Lett. 579 6635 40 16293252 10.1016/j.febslet.2005.10.058 1:CAS:528:DC%2BD2MXht1OlurbP (Pubitemid 41682451)
    • (2005) FEBS Letters , vol.579 , Issue.29 , pp. 6635-6640
    • Fernandez, A.1
  • 15
    • 0030856842 scopus 로고    scopus 로고
    • Protein aggregates seem to play a key role among the parameters influencing the antigenicity of interferon alpha (IFN-α) in normal and transgenic mice
    • DOI 10.1023/A:1012193326789
    • A Braun L Kwee MA Labow J Alsenz 1997 Protein aggregates seem to play a key role among the parameters influencing the antigenicity of interferon alpha (IFN-α) in normal and transgenic mice Pharm Res. 14 1472 8 9358564 10.1023/A:1012193326789 1:CAS:528:DyaK2sXntFehtL0%3D (Pubitemid 27481082)
    • (1997) Pharmaceutical Research , vol.14 , Issue.10 , pp. 1472-1478
    • Braun, A.1    Kwee, L.2    Labow, M.A.3    Alsenz, J.4
  • 16
    • 0027729733 scopus 로고
    • The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation
    • JL Cleland MF Powell SJ Shire 1993 The development of stable protein formulations: a close look at protein aggregation, deamidation, and oxidation Crit Rev Ther Drug. 10 307 77 1:CAS:528:DyaK2cXhsVektro%3D (Pubitemid 24021947)
    • (1993) Critical Reviews in Therapeutic Drug Carrier Systems , vol.10 , Issue.4 , pp. 307-377
    • Cleland, J.L.1    Powell, M.F.2    Shire, S.J.3
  • 17
    • 0036890997 scopus 로고    scopus 로고
    • Immune responses to therapeutic proteins in humans - Clinical significance, assessment and prediction
    • DOI 10.2174/1389201023378175
    • E Koren LA Zuckerman AR Mire-Sluis 2002 Immune responses to therapeutic proteins in humans - clinical significance, assessment and prediction Curr Pharm Biotechnol. 3 349 60 12463417 10.2174/1389201023378175 1:CAS:528: DC%2BD38XovF2qsb8%3D (Pubitemid 35364009)
    • (2002) Current Pharmaceutical Biotechnology , vol.3 , Issue.4 , pp. 349-360
    • Koren, E.1    Zuckerman, L.A.2    Mire-Sluis, A.R.3
  • 18
    • 0027475961 scopus 로고
    • Safety of intravenous immunoglobulin
    • CA Thornton M Ballow 1993 Safety of intravenous immunoglobulin Arch Neurol. 50 135 6 8431130 1:STN:280:DyaK3s7lvFentg%3D%3D (Pubitemid 23054793)
    • (1993) Archives of Neurology , vol.50 , Issue.2 , pp. 135-136
    • Thornton, C.A.1    Ballow, M.2
  • 19
    • 2642550862 scopus 로고    scopus 로고
    • Challenges in the development of high protein concentration formulations
    • DOI 10.1002/jps.20079
    • SJ Shire Z Shahrokh J Liu 2004 Challenges in the development of high protein concentration formulations J Pharm Sci. 93 1390 402 15124199 10.1002/jps.20079 1:CAS:528:DC%2BD2cXks12iurY%3D (Pubitemid 38725014)
    • (2004) Journal of Pharmaceutical Sciences , vol.93 , Issue.6 , pp. 1390-1402
    • Shire, S.J.1    Shahrokh, Z.2    Liu, J.3
  • 20
    • 33749057744 scopus 로고    scopus 로고
    • Protein aggregation and bioprocessing
    • DOI 10.1208/aapsj080366, 66
    • MEM Cromwell E Hilario F Jacobson 2006 Protein aggregation and bioprocessing AAPS Journal. 8 E572 9 17025275 10.1208/aapsj080366 1:CAS:528:DC%2BD28XhtVGltLnJ (Pubitemid 44458092)
    • (2006) AAPS Journal , vol.8 , Issue.3
    • Cromwell, M.E.M.1    Hilario, E.2    Jacobson, F.3
  • 21
    • 55749113694 scopus 로고    scopus 로고
    • Reversible self-association of a concentrated monoclonal antibody solution mediated by Fab-Fab interaction that impacts solution viscosity
    • 18240303 10.1002/jps.21322 1:CAS:528:DC%2BD1cXht1Sgt7rE
    • S Kanai J Liu TW Patapoff SJ Shire 2008 Reversible self-association of a concentrated monoclonal antibody solution mediated by Fab-Fab interaction that impacts solution viscosity J Pharm Sci. 97 4219 27 18240303 10.1002/jps.21322 1:CAS:528:DC%2BD1cXht1Sgt7rE
    • (2008) J Pharm Sci. , vol.97 , pp. 4219-27
    • Kanai, S.1    Liu, J.2    Patapoff, T.W.3    Shire, S.J.4
  • 22
    • 76649099495 scopus 로고    scopus 로고
    • Specific interactions in high concentration antibody solutions resulting in high viscosity
    • 19705420 10.1002/jps.22190 1:CAS:528:DC%2BC3cXmvVCrtQ%3D%3D
    • S Yadav J Liu SJ Shire DS Kalonia 2010 Specific interactions in high concentration antibody solutions resulting in high viscosity J Pharm Sci. 99 1152 68 19705420 10.1002/jps.22190 1:CAS:528:DC%2BC3cXmvVCrtQ%3D%3D
    • (2010) J Pharm Sci. , vol.99 , pp. 1152-68
    • Yadav, S.1    Liu, J.2    Shire, S.J.3    Kalonia, D.S.4
  • 23
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • DOI 10.1021/bp040016j
    • R Jefferis 2005 Glycosylation of recombinant antibody therapeutics Biotechnol Prog. 21 11 6 15903235 10.1021/bp040016j 1:CAS:528:DC%2BD2cXhtFSlurrP (Pubitemid 40218466)
    • (2005) Biotechnology Progress , vol.21 , Issue.1 , pp. 11-16
    • Jefferis, R.1
  • 24
    • 0024615169 scopus 로고
    • Analytical centrifugation with preparative ultracentrifuges
    • 2662806 10.1016/0003-2697(89)90297-2 1:CAS:528:DyaL1MXhsFSlt7o%3D
    • AP Minton 1989 Analytical centrifugation with preparative ultracentrifuges Anal Biochem. 176 209 16 2662806 10.1016/0003-2697(89)90297-2 1:CAS:528:DyaL1MXhsFSlt7o%3D
    • (1989) Anal Biochem. , vol.176 , pp. 209-16
    • Minton, A.P.1
  • 25
    • 0018785999 scopus 로고
    • Macromolecular characterization by sedimentation equilibrium in the preparative ultracentrifuge
    • 758322 1:CAS:528:DyaE1MXotlaqtw%3D%3D
    • RJ Pollet BA Haase ML Standaert 1979 Macromolecular characterization by sedimentation equilibrium in the preparative ultracentrifuge J Biol Chem. 254 30 3 758322 1:CAS:528:DyaE1MXotlaqtw%3D%3D
    • (1979) J Biol Chem. , vol.254 , pp. 30-3
    • Pollet, R.J.1    Haase, B.A.2    Standaert, M.L.3
  • 26
    • 0020668187 scopus 로고
    • The effect of volume occupancy upon the thermodynamic activity of proteins: Some biochemical consequences
    • 6633513 10.1007/BF00673707 1:CAS:528:DyaL3sXlvFSjsbg%3D
    • AP Minton 1983 The effect of volume occupancy upon the thermodynamic activity of proteins: some biochemical consequences Mol Cell Biochem. 55 119 40 6633513 10.1007/BF00673707 1:CAS:528:DyaL3sXlvFSjsbg%3D
    • (1983) Mol Cell Biochem. , vol.55 , pp. 119-40
    • Minton, A.P.1
  • 27
    • 0023369557 scopus 로고
    • Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. II. Two protein components
    • 3620576 10.1002/bip.360260709 1:CAS:528:DyaL2sXlslWrsbg%3D
    • RC Chatelier AP Minton 1987 Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. II. Two protein components Biopolymers. 26 1097 113 3620576 10.1002/bip.360260709 1:CAS:528:DyaL2sXlslWrsbg%3D
    • (1987) Biopolymers. , vol.26 , pp. 1097-113
    • Chatelier, R.C.1    Minton, A.P.2
  • 28
    • 0023322946 scopus 로고
    • Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. I. Self-associating proteins
    • 3567324 10.1002/bip.360260405 1:CAS:528:DyaL2sXkslelur0%3D
    • RC Chatelier AP Minton 1987 Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. I. Self-associating proteins Biopolymers. 26 507 24 3567324 10.1002/bip.360260405 1:CAS:528:DyaL2sXkslelur0%3D
    • (1987) Biopolymers. , vol.26 , pp. 507-24
    • Chatelier, R.C.1    Minton, A.P.2
  • 29
    • 0003363832 scopus 로고
    • Thermodynamics
    • C. Tanford (eds). John Wiley & Sons New York
    • Tanford C. Thermodynamics. In: Tanford C, editor. Physical chemistry of macromolecules. New York: John Wiley & Sons; 1961. p. 180-272.
    • (1961) Physical Chemistry of Macromolecules , pp. 180-272
    • Tanford, C.1
  • 30
    • 0015230398 scopus 로고
    • Equilibrium centrifugation of nonideal systems. The donnan effect in self-associating systems
    • 5119248 10.1021/bi00793a013 1:STN:280:DyaE38%2FktFCisA%3D%3D
    • DE Roark DA Yphantis 1971 Equilibrium centrifugation of nonideal systems. The donnan effect in self-associating systems Biochemistry. 10 3241 9 5119248 10.1021/bi00793a013 1:STN:280:DyaE38%2FktFCisA%3D%3D
    • (1971) Biochemistry. , vol.10 , pp. 3241-9
    • Roark, D.E.1    Yphantis, D.A.2
  • 31
    • 21344472449 scopus 로고    scopus 로고
    • Measurement of fluid viscosity at microliter volumes using quartz impedance analysis
    • Saluja A, Kalonia DS. Measurement of fluid viscosity at microliter volumes using quartz impedance analysis. AAPS PharmSciTech. 2004;5:68-81.
    • (2004) AAPS PharmSciTech , Issue.5 , pp. 68-81
    • Saluja, A.1    Kalonia, D.S.2
  • 32
    • 0001090212 scopus 로고    scopus 로고
    • Viscoelastic properties of low-viscosity liquids studied with thickness-shear mode resonators
    • 10.1021/ac9711798 1:CAS:528:DyaK1cXjsVWruro%3D
    • A Bund G Schwitzgebel 1998 Viscoelastic properties of low-viscosity liquids studied with thickness-shear mode resonators Anal Chem. 70 2584 8 10.1021/ac9711798 1:CAS:528:DyaK1cXjsVWruro%3D
    • (1998) Anal Chem. , vol.70 , pp. 2584-8
    • Bund, A.1    Schwitzgebel, G.2
  • 33
    • 0010379981 scopus 로고
    • The Calculation of Zeta Potential
    • R.H. Ottewill R.L. Rowell (eds). Academic New York
    • Hunter RJ. The Calculation of Zeta Potential. In: Ottewill RH and Rowell RL, editors. Zeta Potential in Colloid Science Principles and Applications. New York: Academic; 1981. p. 59-124.
    • (1981) Zeta Potential in Colloid Science Principles and Applications , pp. 59-124
    • Hunter, R.J.1
  • 35
    • 0011751228 scopus 로고
    • Charge and potential distribution at interface
    • R.H. Ottewill R.L. Rowell (eds). Academic New York
    • Hunter RJ. Charge and potential distribution at interface. In: Ottewill RH and Rowell RL, editors. Zeta potential in colloid science principles and application. New York: Academic; 1981. p. 11-58.
    • (1981) Zeta Potential in Colloid Science Principles and Application , pp. 11-58
    • Hunter, R.J.1
  • 36
    • 17644443266 scopus 로고    scopus 로고
    • Use of T4 lysozyme charge mutants to examine electrophoretic models
    • DOI 10.1016/S0301-4622(02)00168-0, PII S0301462202001680
    • JA Durant C Chen TM Laue TP Moody SA Allison 2002 Use of T4 lysozyme charge mutants to examine electrophoretic models Biophys. Chem. 101-102 593 609 12488029 10.1016/S0301-4622(02)00168-0 (Pubitemid 35462074)
    • (2002) Biophysical Chemistry , vol.101-102 , pp. 593-609
    • Durant, J.A.1    Chen, C.2    Laue, T.M.3    Moody, T.P.4    Allison, S.A.5
  • 37
    • 1642345302 scopus 로고    scopus 로고
    • Nonequilibrium thermodynamics of membrane-confined electrophoresis
    • DOI 10.1016/j.bpc.2003.10.009, PII S0301462203002977
    • TP Moody HK Shepard 2004 Nonequilibrium thermodynamics of membrane-confined electrophoresis Biophys Chem. 108 51 76 15043921 10.1016/j.bpc.2003.10.009 1:CAS:528:DC%2BD2cXisVens78%3D (Pubitemid 38388481)
    • (2004) Biophysical Chemistry , vol.108 , Issue.1-3 , pp. 51-76
    • Moody, T.P.1    Shepard, H.K.2
  • 40
    • 11144267761 scopus 로고    scopus 로고
    • Valence and anion binding of bovine ribonuclease A between pH 6 and 8
    • DOI 10.1016/j.ab.2004.09.009, PII S0003269704007316
    • TP Moody JS Kingsbury JA Durant TJ Wilson SF Chase TM Laue 2005 Valence and anion binding of bovine ribonuclease A between pH 6 and 8 Anal Biochem. 336 243 52 15620889 10.1016/j.ab.2004.09.009 1:CAS:528:DC%2BD2cXhtFGiu7nN (Pubitemid 40038022)
    • (2005) Analytical Biochemistry , vol.336 , Issue.2 , pp. 243-252
    • Moody, T.P.1    Kingsbury, J.S.2    Durant, J.A.3    Wilson, T.J.4    Chase, S.F.5    Laue, T.M.6
  • 41
    • 0017380736 scopus 로고
    • Electrical double layer, zeta potential, and electrophoretic charge of double stranded DNA
    • JA Schellman D Stigter 1977 Electrical double layer, zeta potential, and electrophoretic charge of double-stranded DNA Biopolymers. 16 1415 34 880365 10.1002/bip.1977.360160704 1:CAS:528:DyaE2sXks1Chsbo%3D (Pubitemid 8110410)
    • (1977) Biopolymers , vol.16 , Issue.7 , pp. 1415-1434
    • Schellman, J.A.1
  • 42
    • 33846140780 scopus 로고    scopus 로고
    • Antibody structure, instability, and formulation
    • DOI 10.1002/jps.20727
    • W Wang S Singh DL Zeng K King S Nema 2007 Antibody structure, instability, and formulation J Pharm Sci. 96 1 26 16998873 10.1002/jps.20727 1:CAS:528:DC%2BD2sXivFCjtA%3D%3D (Pubitemid 46087335)
    • (2007) Journal of Pharmaceutical Sciences , vol.96 , Issue.1 , pp. 1-26
    • Wang, W.1    Singh, S.2    Zeng, D.L.3    King, K.4    Nema, S.5
  • 43
    • 17644421429 scopus 로고    scopus 로고
    • Dynamic light scattering application to study protein interactions in electrolyte solutions
    • DOI 10.1007/s10867-004-0997-z
    • S Li D Xing J Li 2004 Dynamic light scattering application to study protein interactions in electrolyte solutions J Biol Phys. 30 313 24 10.1007/s10867-004-0997-z 1:CAS:528:DC%2BD2MXht1Ojurw%3D (Pubitemid 40558065)
    • (2004) Journal of Biological Physics , vol.30 , Issue.4 , pp. 313-324
    • Li, S.1    Xing, D.2    Li, J.3
  • 44
    • 77957843464 scopus 로고    scopus 로고
    • Intermolecular interactions of IgG1 monoclonal antibodies at high concentrations characterized by light scattering
    • Scherer TM, Liu J, Shire SJ, Minton AP. Intermolecular interactions of IgG1 monoclonal antibodies at high concentrations characterized by light scattering. J Phys Chem B. 2010;114:12948-12957.
    • (2010) J Phys Chem B , vol.114 , pp. 12948-12957
    • Scherer, T.M.1    Liu, J.2    Shire, S.J.3    Minton, A.P.4
  • 45
    • 37049103677 scopus 로고
    • Viscoelastic properties of concentrated latices: Part 1. - Methods of examination
    • 10.1039/f19827802873 1:CAS:528:DyaL38XlvFyrs74%3D
    • R Buscall JW Goodwin MW Hawkins RH Ottewill 1982 Viscoelastic properties of concentrated latices: part 1. - methods of examination J Chem Soc, Faraday Trans 1 F. 78 2873 87 10.1039/f19827802873 1:CAS:528:DyaL38XlvFyrs74%3D
    • (1982) J Chem Soc, Faraday Trans 1 F. , vol.78 , pp. 2873-87
    • Buscall, R.1    Goodwin, J.W.2    Hawkins, M.W.3    Ottewill, R.H.4
  • 46
    • 37049112458 scopus 로고
    • Viscoelastic properties of concentrated latices: Part 2. - Theoretical analysis
    • 10.1039/f19827802889 1:CAS:528:DyaL38XlvFyrs78%3D
    • R Buscall JW Goodwin MW Hawkins RH Ottewill 1982 Viscoelastic properties of concentrated latices: part 2. - Theoretical analysis J Chem Soc, Faraday Trans 1 F. 78 2889 99 10.1039/f19827802889 1:CAS:528:DyaL38XlvFyrs78%3D
    • (1982) J Chem Soc, Faraday Trans 1 F. , vol.78 , pp. 2889-99
    • Buscall, R.1    Goodwin, J.W.2    Hawkins, M.W.3    Ottewill, R.H.4
  • 47
    • 0016898816 scopus 로고
    • Second electroviscous effect in polymer latices
    • 10.1122/1.549428
    • IM Kriegerand M Eguiluz 1976 Second electroviscous effect in polymer latices Trans Soc Rheol. 20 29 45 10.1122/1.549428
    • (1976) Trans Soc Rheol. , vol.20 , pp. 29-45
    • Kriegerand, I.M.1    Eguiluz, M.2
  • 48
    • 77149128116 scopus 로고    scopus 로고
    • Formation of the dynamic clusters in concentrated Lysozyme protein solutions
    • 10.1021/jz900127c 1:CAS:528:DC%2BD1MXhtl2qu7nN
    • L Porcar P Falus WR Chen A Faraone E Fratini K Hong, et al. 2010 Formation of the dynamic clusters in concentrated Lysozyme protein solutions J Phys Chem Lett. 1 126 9 10.1021/jz900127c 1:CAS:528:DC%2BD1MXhtl2qu7nN
    • (2010) J Phys Chem Lett. , vol.1 , pp. 126-9
    • Porcar, L.1    Falus, P.2    Chen, W.R.3    Faraone, A.4    Fratini, E.5    Hong, K.6
  • 51
    • 77953787610 scopus 로고    scopus 로고
    • Observation of a large-scale superstructure in concentrated hemoglobin solutions by using small angle neutron scattering
    • 10.1021/jz100576c 1:CAS:528:DC%2BC3cXms1ShsbY%3D
    • AM Stadler R Schweins G Zaccai P Lindner 2010 Observation of a large-scale superstructure in concentrated hemoglobin solutions by using small angle neutron scattering J Phys Chem Lett. 1 1805 8 10.1021/jz100576c 1:CAS:528:DC%2BC3cXms1ShsbY%3D
    • (2010) J Phys Chem Lett. , vol.1 , pp. 1805-8
    • Stadler, A.M.1    Schweins, R.2    Zaccai, G.3    Lindner, P.4
  • 52
    • 9644259209 scopus 로고    scopus 로고
    • Equilibrium cluster formation in concentrated protein solutions and colloids
    • DOI 10.1038/nature03109
    • A Stradner H Sedgwick F Cardinaux WCK Poon SU Egelhaaf P Schurtenberger 2004 Equilibrium cluster formation in concentrated protein solutions and colloids Nature. 432 492 5 15565151 10.1038/nature03109 1:CAS:528: DC%2BD2cXhtVWitbnI (Pubitemid 39576527)
    • (2004) Nature , vol.432 , Issue.7016 , pp. 492-495
    • Stradner, A.1    Sedgwick, H.2    Cardinaux, F.3    Poon, W.C.K.4    Egelhaaf, S.U.5    Schurtenberger, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.