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>Quantitative Characterization of Weak Self-Association in Concentrated Solutions of Immunoglobulin G via the Measurement of Sedimentation Equilibrium and Osmotic Pressure
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Quantitative Characterization of Weak Self-Association in Concentrated Solutions of Immunoglobulin G via the Measurement of Sedimentation Equilibrium and Osmotic Pressure
The sedimentation equilibrium of solutions of immunoglobulin G in saline buffer, over a concentration range up to 125 g/L, was measured and analyzed in the context of a model that takes into account the possibility of attractive intermolecular interaction leading to the reversible formation of oligomeric species and repulsive intermolecular interaction leading to nonideal solution behavior. Additionally, previously published data on the concentration dependence of the osmotic pressure of immunoglobulin G under similar conditions, over a concentration range up to 400 g/L, were analyzed in the context of a newly developed thermodynamic formalism describing the osmotic pressure of a solution containing multiple nondiffusible solute species at an arbitrary concentration. Both sets of data are quantitatively accounted for by a model in which IgG self-associates at very high concentration to form (predominantly) trimers under the conditions of these experiments.
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机译：在模型范围内测量并分析了免疫球蛋白G在盐水缓冲液中浓度高达125 g / L的溶液的沉降平衡，该模型考虑了有吸引力的分子间相互作用导致寡聚体可逆形成的可能性物种和排斥性分子间相互作用导致非理想溶液行为。此外，在新开发的热力学形式主义的背景下，分析了以前发表的关于免疫球蛋白G在类似条件下，浓度范围高达400 g / L的渗透压的浓度依赖性的数据，描述了含有任意浓度的多种不可扩散溶质物种。在该实验条件下，其中IgG以非常高的浓度自缔合形成（主要是）三聚体的模型对这两组数据进行了定量说明。
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