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Volumn 377, Issue 2, 2008, Pages 128-133

Corrigendum to "Measurement of the second osmotic virial coefficient for protein solutions exhibiting monomer-dimer equilibrium" [Anal. Biochem. 377 (2008) 128-133] (DOI:10.1016/j.ab.2008.03.032);Measurement of the second osmotic virial coefficient for protein solutions exhibiting monomer-dimer equilibrium

Author keywords

Concentrated protein formulations; Low angle light scattering; Self association

Indexed keywords

ASSOCIATION REACTIONS; LIGHT SCATTERING; MONOMERS; OSMOSIS; PROTEINS;

EID: 43049095653     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.08.007     Document Type: Erratum
Times cited : (49)

References (18)
  • 1
    • 0001279457 scopus 로고
    • Predicting protein crystallization from a dilute-solution property
    • A. George W.W. Wilson Predicting protein crystallization from a dilute-solution property Acta Crystallogr. Sect. D 50 1994 361 365
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 361-365
    • George, A.1    Wilson, W.W.2
  • 2
    • 34247644354 scopus 로고    scopus 로고
    • Nonequivalence of second virial coefficients from sedimentation equilibrium and static light scattering studies of protein solutions
    • D.J. Winzor M. Deszczynski S.E. Harding P.R. Wills Nonequivalence of second virial coefficients from sedimentation equilibrium and static light scattering studies of protein solutions Biophys. Chem. 128 2007 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
  • 3
    • 33644683427 scopus 로고    scopus 로고
    • Negative second virial coefficients as predictors of protein crystal growth: evidence from sedimentation equilibrium studies that refutes the designation of those light scattering parameters as osmotic virial coefficients
    • M. Deszczynski S.E. Harding D.J. Winzor Negative second virial coefficients as predictors of protein crystal growth: evidence from sedimentation equilibrium studies that refutes the designation of those light scattering parameters as osmotic virial coefficients Biophys. Chem. 120 2006 106 113
    • (2006) Biophys. Chem. , vol.120 , pp. 106-113
    • Deszczynski, M.1    Harding, S.E.2    Winzor, D.J.3
  • 4
    • 0242515822 scopus 로고    scopus 로고
    • Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor
    • E.Y. Chi S. Krishnan B.S. Kendrick B.S. Chang J.F. Carpenter T.W. Randolph Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor Protein Sci. 12 2003 903 913
    • (2003) Protein Sci. , vol.12 , pp. 903-913
    • Chi, E.Y.1    Krishnan, S.2    Kendrick, B.S.3    Chang, B.S.4    Carpenter, J.F.5    Randolph, T.W.6
  • 5
    • 26844533680 scopus 로고    scopus 로고
    • Composition gradient static light scattering: a new technique for rapid detection and quantitative characterization of reversible macromolecular hetero-associations in solution
    • A.K. Attri A.P. Minton Composition gradient static light scattering: a new technique for rapid detection and quantitative characterization of reversible macromolecular hetero-associations in solution Anal. Biochem. 346 2005 132 138
    • (2005) Anal. Biochem. , vol.346 , pp. 132-138
    • Attri, A.K.1    Minton, A.P.2
  • 6
    • 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
    • A.K. Attri A.P. Minton New methods for measuring macromolecular interactions in solution via static light scattering: basic methodology, and application to nonassociating and self-associating proteins Anal. Biochem. 337 2005 103 110
    • (2005) Anal. Biochem. , vol.337 , pp. 103-110
    • Attri, A.K.1    Minton, A.P.2
  • 7
    • 10044279535 scopus 로고    scopus 로고
    • Determination of second virial coefficient of proteins using a dual-detector cell for simultaneous measurement of scattered light intensity and concentration in SEC-HPLC
    • H. Bajaj V.K. Sharma D.S. Kalonia Determination of second virial coefficient of proteins using a dual-detector cell for simultaneous measurement of scattered light intensity and concentration in SEC-HPLC Biophys. J. 87 2004 4048 4055
    • (2004) Biophys. J. , vol.87 , pp. 4048-4055
    • Bajaj, H.1    Sharma, V.K.2    Kalonia, D.S.3
  • 8
    • 7744225246 scopus 로고
    • The association of insulin: I. Preliminary investigations
    • P. Doty M. Gellert B. Rabinovitch The association of insulin: I. Preliminary investigations J. Am. Chem. Soc. 74 1952 2065 2069
    • (1952) J. Am. Chem. Soc. , vol.74 , pp. 2065-2069
    • Doty, P.1    Gellert, M.2    Rabinovitch, B.3
  • 9
    • 0000819133 scopus 로고
    • Molecular interactions in β-lactoglobulin: III. Light scattering investigation of the stoichiometry of the association between pH 3.7 and 5.2
    • R. Townend S.N. Timasheff Molecular interactions in β -lactoglobulin: III. Light scattering investigation of the stoichiometry of the association between pH 3.7 and 5.2 J. Am. Chem. Soc. 82 1960 3168 3174
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 3168-3174
    • Townend, R.1    Timasheff, S.N.2
  • 10
    • 0000819132 scopus 로고
    • Molecular interactions in β -lactoglobulin: IV. The dissociation of β-lactoglobulin below pH 3.5
    • R. Townend L. Weinberger S.N. Timasheff Molecular interactions in β -lactoglobulin: IV. The dissociation of β -lactoglobulin below pH 3.5 J. Am. Chem. Soc. 82 1960 3175 3179
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 3175-3179
    • Townend, R.1    Weinberger, L.2    Timasheff, S.N.3
  • 11
    • 0004283386 scopus 로고    scopus 로고
    • Principles of Colloid and Surface Chemistry
    • P.C. Hiemenz R. Rajagopalan Principles of Colloid and Surface Chemistry 3rd ed. 1997 Marcel Dekker New York
    • (1997)
    • Hiemenz, P.C.1    Rajagopalan, R.2
  • 12
    • 0031768735 scopus 로고    scopus 로고
    • Protein interactions in solution characterized by light and neutron scattering: comparison of lysozyme and chymotrypsinogen
    • O.D. Velev E.W. Kaler A.M. Lenhoff Protein interactions in solution characterized by light and neutron scattering: comparison of lysozyme and chymotrypsinogen Biophys. J. 75 1998 2682 2697
    • (1998) Biophys. J. , vol.75 , pp. 2682-2697
    • Velev, O.D.1    Kaler, E.W.2    Lenhoff, A.M.3
  • 13
    • 85120281161 scopus 로고    scopus 로고
    • Polymer–polymer interactions in dilute solutions
    • J. Selser Polymer–polymer interactions in dilute solutions W. Brown Light Scattering Principles and Development 1996 Clarendon Press Oxford 232 254
    • (1996) , pp. 232-254
    • Selser, J.1
  • 15
    • 0030272655 scopus 로고    scopus 로고
    • The effect of temperature and ionic strength on the dimerisation of beta-lactoglobulin
    • P. Aymard D. Durand T. Nicolai The effect of temperature and ionic strength on the dimerisation of beta-lactoglobulin Int. J. Biol. Macromol. 19 1996 213 221
    • (1996) Int. J. Biol. Macromol. , vol.19 , pp. 213-221
    • Aymard, P.1    Durand, D.2    Nicolai, T.3
  • 16
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultra-centrifuge by non-linear least-squares techniques
    • M.L. Johnson J.J. Correia D.A. Yphantis H.R. Halvorson Analysis of data from the analytical ultra-centrifuge by non-linear least-squares techniques Biophys. J. 36 1981 575 588
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 17
    • 52449112053 scopus 로고    scopus 로고
    • High concentration formulations of recombinant human interleukin-1 receptor antagonist: II. Aggregation kinetics
    • J.R. Alford B.S. Kendrick J.F. Carpenter T.W. Randolph High concentration formulations of recombinant human interleukin-1 receptor antagonist: II. Aggregation kinetics J. Pharm. Sci. 2007 10.1002/jps.21205
    • (2007) J. Pharm. Sci.
    • Alford, J.R.1    Kendrick, B.S.2    Carpenter, J.F.3    Randolph, T.W.4
  • 18
    • 0031723926 scopus 로고    scopus 로고
    • Molecular origins of osmotic second virial coefficients of proteins
    • B.L. Neal D. Asthagiri A.M. Lenhoff Molecular origins of osmotic second virial coefficients of proteins Biophys. J. 75 1998 2469 2477
    • (1998) Biophys. J. , vol.75 , pp. 2469-2477
    • Neal, B.L.1    Asthagiri, D.2    Lenhoff, A.M.3


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