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Volumn 96, Issue 5, 2009, Pages 1992-1998

Static light scattering from concentrated protein solutions II: Experimental test of theory for protein mixtures and weakly self-associating proteins

Author keywords

[No Author keywords available]

Indexed keywords

BOVINE SERUM ALBUMIN; CHYMOTRYPSIN A; DIMER; MONOMER; OVALBUMIN; OVOMUCOID; PROTEIN; ALPHA-CHYMOTRYPSIN; CHYMOTRYPSIN;

EID: 65549164345     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2008.11.054     Document Type: Article
Times cited : (62)

References (36)
  • 1
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: Biochemical, biophysical and potential physiological consequences
    • Zhou, H. -X., G. Rivas, and A. P. Minton. 2008. Macromolecular crowding and confinement: biochemical, biophysical and potential physiological consequences. Ann. Rev. Biophys. 37:375-397.
    • (2008) Ann. Rev. Biophys , vol.37 , pp. 375-397
    • Zhou, H.-X.1    Rivas, G.2    Minton, A.P.3
  • 2
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical, and physiological consequences
    • Zimmerman, S. B., and A. P. Minton. 1993. Macromolecular crowding: biochemical, biophysical, and physiological consequences. Annu. Rev. Biophys. Biomol. Struct. 22:27-65.
    • (1993) Annu. Rev. Biophys. Biomol. Struct , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 3
    • 2642550862 scopus 로고    scopus 로고
    • Challenges in the development of high protein concentration formulations
    • Shire, S. J., Z. Shahrokh, and J. Liu. 2004. Challenges in the development of high protein concentration formulations. J. Pharm. Sci. 93:1390-1402.
    • (2004) J. Pharm. Sci , vol.93 , pp. 1390-1402
    • Shire, S.J.1    Shahrokh, Z.2    Liu, J.3
  • 4
    • 0017381152 scopus 로고
    • Analysis of nonideal behavior in concentrated hemoglobin solutions
    • Ross, P. D., and A. P. Minton. 1977. Analysis of nonideal behavior in concentrated hemoglobin solutions. J. Mol. Biol. 112:437-452.
    • (1977) J. Mol. Biol , vol.112 , pp. 437-452
    • Ross, P.D.1    Minton, A.P.2
  • 5
    • 34447504216 scopus 로고    scopus 로고
    • Static light scattering from concentrated protein solutions I. General theory for protein mixtures and application to self-associating proteins
    • Minton, A. P. 2007. Static light scattering from concentrated protein solutions I. General theory for protein mixtures and application to self-associating proteins. Biophys. J. 93:1321-1328.
    • (2007) Biophys. J , vol.93 , pp. 1321-1328
    • Minton, A.P.1
  • 6
    • 38149048416 scopus 로고    scopus 로고
    • The effective hard particle model provides a simple, robust, and broadly applicable description of nonideal behavior in concentrated solutions of bovine serum albumin and other nonassociating proteins
    • Minton, A. P. 2007. The effective hard particle model provides a simple, robust, and broadly applicable description of nonideal behavior in concentrated solutions of bovine serum albumin and other nonassociating proteins. J. Pharm. Sci. 96:3466-3469.
    • (2007) J. Pharm. Sci , vol.96 , pp. 3466-3469
    • Minton, A.P.1
  • 7
    • 41649094226 scopus 로고    scopus 로고
    • Effective hard particle model for the osmotic pressure of highly concentrated binary protein solutions
    • Minton, A. P. 2008. Effective hard particle model for the osmotic pressure of highly concentrated binary protein solutions. Biophys. J. 94:L57-L59.
    • (2008) Biophys. J , vol.94
    • Minton, A.P.1
  • 8
    • 84985721961 scopus 로고
    • Light scattering of bovine serum albumin solutions: Extension of the hard particle model to allow for electrostatic repulsion
    • Minton, A. P., and H. Edelhoch. 1982. Light scattering of bovine serum albumin solutions: extension of the hard particle model to allow for electrostatic repulsion. Biopolymers. 21:451-458.
    • (1982) Biopolymers , vol.21 , pp. 451-458
    • Minton, A.P.1    Edelhoch, H.2
  • 9
    • 0033587619 scopus 로고    scopus 로고
    • Direct observation of the self-association of dilute proteins in the presence of inert macromolecules at high concentration via tracer sedimentation equilibrium: Theory, experiment, and biological significance
    • Rivas, G., J. A. Fernandez, and A. P. Minton. 1999. Direct observation of the self-association of dilute proteins in the presence of inert macromolecules at high concentration via tracer sedimentation equilibrium: theory, experiment, and biological significance. Biochemistry. 38:9379-9388.
    • (1999) Biochemistry , vol.38 , pp. 9379-9388
    • Rivas, G.1    Fernandez, J.A.2    Minton, A.P.3
  • 10
    • 0018175121 scopus 로고
    • Temperature dependence of nonideality in concentrated solutions of hemoglobin
    • Ross, P. D., R. W. Briehl, and A. P. Minton. 1978. Temperature dependence of nonideality in concentrated solutions of hemoglobin. Biopolymers. 17:2285-2288.
    • (1978) Biopolymers , vol.17 , pp. 2285-2288
    • Ross, P.D.1    Briehl, R.W.2    Minton, A.P.3
  • 11
    • 0028822574 scopus 로고
    • A molecular model for the dependence of the osmotic pressure of bovine serum albumin upon concentration and pH
    • Minton, A. P. 1995. A molecular model for the dependence of the osmotic pressure of bovine serum albumin upon concentration and pH. Biophys. Chem. 57:65-70.
    • (1995) Biophys. Chem , vol.57 , pp. 65-70
    • Minton, A.P.1
  • 12
    • 50249139548 scopus 로고    scopus 로고
    • Automated measurement of the static light scattering of macromolecular solutions over a broad range of concentrations
    • Fernández, C., and A. P. Minton. 2008. Automated measurement of the static light scattering of macromolecular solutions over a broad range of concentrations. Anal. Biochem. 381:254-257.
    • (2008) Anal. Biochem , vol.381 , pp. 254-257
    • Fernández, C.1    Minton, A.P.2
  • 13
    • 0014143995 scopus 로고
    • Dimerization and activity of chymotrypsin at pH 4
    • Morimoto, K., and G. Kegeles. 1967. Dimerization and activity of chymotrypsin at pH 4. Biochemistry. 6:3007-3010.
    • (1967) Biochemistry , vol.6 , pp. 3007-3010
    • Morimoto, K.1    Kegeles, G.2
  • 14
    • 0015242084 scopus 로고
    • Dimerization of alpha-chymotrypsin I. pH dependence in the acid region
    • Aune, K., and S. N. Timasheff. 1971. Dimerization of alpha-chymotrypsin I. pH dependence in the acid region. Biochemistry. 10:1609-1617.
    • (1971) Biochemistry , vol.10 , pp. 1609-1617
    • Aune, K.1    Timasheff, S.N.2
  • 15
    • 33645984885 scopus 로고    scopus 로고
    • Rapid quantitative characterization of protein interactions by composition gradient static light scattering
    • Kameyama, K., and A. P. Minton. 2006. Rapid quantitative characterization of protein interactions by composition gradient static light scattering. Biophys. J. 90:2164-2169.
    • (2006) Biophys. J , vol.90 , pp. 2164-2169
    • Kameyama, K.1    Minton, A.P.2
  • 16
    • 0004521272 scopus 로고
    • 1% values for proteins at selected wavelengths in the ultraviolet and visible region
    • Biology. G. D. Fasman, editor. CRC Press, Cleveland, pp
    • 1% values for proteins at selected wavelengths in the ultraviolet and visible region. In Handbook of Biochemistry and Molecular Biology. G. D. Fasman, editor. CRC Press, Cleveland, pp. 383-545.
    • (1976) Handbook of Biochemistry and Molecular , pp. 383-545
    • Kirschenbaum, D.M.1
  • 17
    • 0015210966 scopus 로고
    • Batch purification of ovomucoid and characterization of the purified product
    • Davis, J. G., C. J. Mapes, and J. W. Donovan. 1971. Batch purification of ovomucoid and characterization of the purified product. Biochemistry. 10:39-42.
    • (1971) Biochemistry , vol.10 , pp. 39-42
    • Davis, J.G.1    Mapes, C.J.2    Donovan, J.W.3
  • 18
    • 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
    • Attri, A. K., and A. P. Minton. 2005. New methods for measuring macromolecular interactions in solution via static light scattering: basic methodology and application to nonassociating and self-associating proteins. Anal. Biochem. 337:103-110.
    • (2005) Anal. Biochem , vol.337 , pp. 103-110
    • Attri, A.K.1    Minton, A.P.2
  • 19
    • 85031356227 scopus 로고    scopus 로고
    • Theisen, A., C. Johann, M. P. Deacon, and S. E. Harding. 2000. Refractive Increment Data-book. Nottingham University Press, Nottingham. 55.
    • Theisen, A., C. Johann, M. P. Deacon, and S. E. Harding. 2000. Refractive Increment Data-book. Nottingham University Press, Nottingham. 55.
  • 21
    • 0002628768 scopus 로고
    • Light scattering in multi-component systems
    • Stockmayer, W. H. 1950. Light scattering in multi-component systems. J. Chem. Phys. 18:58-61.
    • (1950) J. Chem. Phys , vol.18 , pp. 58-61
    • Stockmayer, W.H.1
  • 22
    • 17844405882 scopus 로고    scopus 로고
    • A consistent experimental and modeling approach to light-scattering studies of protein-protein interactions in solution
    • Asthagiri, D., A. Paliwal, D. Abras, A. M. Lenhoff, and M. E. Paulitis. 2005. A consistent experimental and modeling approach to light-scattering studies of protein-protein interactions in solution. Biophys. J. 88:3300-3309.
    • (2005) Biophys. J , vol.88 , pp. 3300-3309
    • Asthagiri, D.1    Paliwal, A.2    Abras, D.3    Lenhoff, A.M.4    Paulitis, M.E.5
  • 23
    • 34247644354 scopus 로고    scopus 로고
    • Nonequivalence of second virial coefficients from sedimentation equilibrium and static light scattering studies of protein solutions
    • Winzor, D. J., M. Deszczynski, S. E. Harding, and P. R. Wills. 2007. Nonequivalence of second virial coefficients from sedimentation equilibrium and static light scattering studies of protein solutions. Biophys. Chem. 128:46-55.
    • (2007) Biophys. Chem , vol.128 , pp. 46-55
    • Winzor, D.J.1    Deszczynski, M.2    Harding, S.E.3    Wills, P.R.4
  • 24
    • 0041931122 scopus 로고    scopus 로고
    • Macromolecular crowding: Qualitative and semiquantitative successes, quantitative challenges
    • Hall, D., and A. P. Minton. 2003. Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges. Biochem. Biophys. Res. Commun. 1649:127-139.
    • (2003) Biochem. Biophys. Res. Commun , vol.1649 , pp. 127-139
    • Hall, D.1    Minton, A.P.2
  • 25
    • 33645087051 scopus 로고
    • Statistical thermodynamics of convex molecule fluids
    • Boublík, T. 1974. Statistical thermodynamics of convex molecule fluids. Mol. Phys. 27:1415-1427.
    • (1974) Mol. Phys , vol.27 , pp. 1415-1427
    • Boublík, T.1
  • 27
    • 0015829813 scopus 로고
    • Theory of aggregation in solution I. General equations and application to the stacking of bases, nucleosides, etc
    • Hill, T. L., and Y. -D. Chen. 1973. Theory of aggregation in solution I. General equations and application to the stacking of bases, nucleosides, etc. Biopolymers. 12:1285-1312.
    • (1973) Biopolymers , vol.12 , pp. 1285-1312
    • Hill, T.L.1    Chen, Y.-D.2
  • 28
    • 0024642066 scopus 로고
    • Hidden self-association of proteins
    • Muramatsu, N., and A. P. Minton. 1989. Hidden self-association of proteins. J. Mol. Recognit. 1:166-171.
    • (1989) J. Mol. Recognit , vol.1 , pp. 166-171
    • Muramatsu, N.1    Minton, A.P.2
  • 29
    • 34848814457 scopus 로고    scopus 로고
    • A high-throughput method for detection of protein self-association and second virial coefficient using size-exclusion chromatography through simultaneouls measurement of concentration and scattered light intensity
    • Bajaj, H., V. K. Sharma, and D. S. Kalonia. 2007. A high-throughput method for detection of protein self-association and second virial coefficient using size-exclusion chromatography through simultaneouls measurement of concentration and scattered light intensity. Pharm. Res. 24:2071-2083.
    • (2007) Pharm. Res , vol.24 , pp. 2071-2083
    • Bajaj, H.1    Sharma, V.K.2    Kalonia, D.S.3
  • 30
    • 52449087976 scopus 로고    scopus 로고
    • High concentration formulations of recombinant human interleukin-1 receptor antagonist: I. Physical characterization
    • Alford, J. R., S. C. Kwok, J. N. Roberts, D. S. Wuttke, B. S. Kendrick, et al. 2008. High concentration formulations of recombinant human interleukin-1 receptor antagonist: I. Physical characterization. J. Pharm. Sci. 97:3035-3050.
    • (2008) J. Pharm. Sci , vol.97 , pp. 3035-3050
    • Alford, J.R.1    Kwok, S.C.2    Roberts, J.N.3    Wuttke, D.S.4    Kendrick, B.S.5
  • 31
    • 1642285049 scopus 로고    scopus 로고
    • Sedimentation equilibrium in a solution containing an arbitrary number of solute species at arbitrary concentrations: Theory and application to concentrated solutions of ribonuclease
    • Zorrilla, S., M. Jiménez, P. Lillo, G. Rivas, and A. P. Minton. 2004. Sedimentation equilibrium in a solution containing an arbitrary number of solute species at arbitrary concentrations: theory and application to concentrated solutions of ribonuclease. Biophys. Chem. 108:89-100.
    • (2004) Biophys. Chem , vol.108 , pp. 89-100
    • Zorrilla, S.1    Jiménez, M.2    Lillo, P.3    Rivas, G.4    Minton, A.P.5
  • 32
    • 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
    • Jiménez, M., G. Rivas, and A. P. Minton. 2007. Quantitative characterization of weak self-association in concentrated solutions of Immunoglobulin G via the measurement of sedimentation equilibrium and osmotic pressure. Biochemistry. 46:8373-8378.
    • (2007) Biochemistry , vol.46 , pp. 8373-8378
    • Jiménez, M.1    Rivas, G.2    Minton, A.P.3
  • 33
    • 0015949065 scopus 로고
    • Studies on self-association of proteins. The self-association of alpha-chymotrypsin at pH 8.3 and ionic strength 0.05
    • Pandit, M. W., and M. S. Narasinga Rao. 1974. Studies on self-association of proteins. The self-association of alpha-chymotrypsin at pH 8.3 and ionic strength 0.05. Biochemistry. 13:1048-1055.
    • (1974) Biochemistry , vol.13 , pp. 1048-1055
    • Pandit, M.W.1    Narasinga Rao, M.S.2
  • 34
    • 78651184423 scopus 로고
    • Determination of stoichiometry and equilibrium constants for reversibly associating systems by molecular sieve chromatography
    • Ackers, G. K., and T. E. Thompson. 1965. Determination of stoichiometry and equilibrium constants for reversibly associating systems by molecular sieve chromatography. Proc. Natl. Acad. Sci. USA. 53:342-349.
    • (1965) Proc. Natl. Acad. Sci. USA , vol.53 , pp. 342-349
    • Ackers, G.K.1    Thompson, T.E.2
  • 35
    • 0018171749 scopus 로고
    • Isoelectric points of proteins: A table
    • Malamud, D., and J. W. Drysdale. 1978. Isoelectric points of proteins: a table. Anal. Biochem. 86:620-647.
    • (1978) Anal. Biochem , vol.86 , pp. 620-647
    • Malamud, D.1    Drysdale, J.W.2
  • 36
    • 0001730934 scopus 로고
    • Analysis, fractionation and purification of egg white proteins with cellulose-cation exchanger
    • Rhodes, M. B., P. R. Azari, and R. E. Feeney. 1958. Analysis, fractionation and purification of egg white proteins with cellulose-cation exchanger. J. Biol. Chem. 230:399-408.
    • (1958) J. Biol. Chem , vol.230 , pp. 399-408
    • Rhodes, M.B.1    Azari, P.R.2    Feeney, R.E.3


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