Characterizing Reversible Protein Association at Moderately High Concentration Via Composition-Gradient Static Light Scattering.

[1]  Reza Esfandiary,et al.  Mechanism of reversible self-association of a monoclonal antibody: role of electrostatic and hydrophobic interactions. , 2015, Journal of pharmaceutical sciences.

[2]  D. Some.  Light-scattering-based analysis of biomolecular interactions , 2013, Biophysical Reviews.

[3]  J. Casas-Finet,et al.  A systematic multitechnique approach for detection and characterization of reversible self-association during formulation development of therapeutic antibodies. , 2013, Journal of pharmaceutical sciences.

[4]  A. Minton,et al.  Intermolecular interactions of IgG1 monoclonal antibodies at high concentrations characterized by light scattering. , 2010, The journal of physical chemistry. B.

[5]  A. Minton,et al.  Static light scattering from concentrated protein solutions II: experimental test of theory for protein mixtures and weakly self-associating proteins. , 2009, Biophysical journal.

[6]  Yatin R. Gokarn,et al.  Ion‐specific modulation of protein interactions: Anion‐induced, reversible oligomerization of a fusion protein , 2008, Protein science : a publication of the Protein Society.

[7]  A. Minton.  Static light scattering from concentrated protein solutions, I: General theory for protein mixtures and application to self-associating proteins. , 2007, Biophysical journal.

[8]  A. Minton,et al.  Rapid quantitative characterization of protein interactions by composition gradient static light scattering. , 2006, Biophysical journal.

[9]  A. Minton,et al.  New methods for measuring macromolecular interactions in solution via static light scattering: basic methodology and application to nonassociating and self-associating proteins. , 2005, Analytical biochemistry.

[10]  Damien Hall,et al.  Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges. , 2003, Biochimica et biophysica acta.

[11]  A. Minton,et al.  Molecular crowding: analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion. , 1998, Methods in enzymology.

[12]  D. Winzor,et al.  Thermodynamic nonideality in macromolecular solutions. Evaluation of parameters for the prediction of covolume effects. , 1990, European journal of biochemistry.

[13]  A. Minton,et al.  Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. I. Self‐associating proteins , 1987, Biopolymers.

[14]  A. Minton,et al.  Light scattering of bovine serum albumin solutions: Extension of the hard particle model to allow for electrostatic repulsion , 1982 .

[15]  T. Boublı́k.  Statistical thermodynamics of convex molecule fluids , 1974 .

[16]  W. Stockmayer.  Light Scattering in Multi‐Component Systems , 1950 .