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In relation to this article, we declare that there is no conflict of interest.
Publication history
Received January 11, 2009
Accepted February 17, 2009
articles This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Salt-induced protein separation in an aqueous electrolyte solution

Division of Chemical Engineering and Molecular Thermodynamics Laboratory, Hanyang University, Seoul 133-791, Korea
Korean Journal of Chemical Engineering, September 2009, 26(5), 1365-1372(8), 10.1007/s11814-009-0211-x
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Abstract

Liquid-liquid phase separations of aqueous ovalbumin and bovine serum albumin (BSA) solutions are reported experimentally for a wide range of solution conditions. The temperature-induced clouding of protein solutions, which signals the onset of liquid-liquid phase separation, provides a simple means of assessing the effect of solution conditions on the strength of protein interaction. Our results show that the effect of salts on protein interactions depends sensitively on the ionic composition of solution and the identities of both the cation and the anion of the added_x000D_ salts. The results are used to test and refine theoretical models for the interaction energy between macromolecules. A modified perturbed hard-sphere chain (MPHSC) model is employed to determine the interaction energy for solvation forces playing an important role in protein interactions and to predict the osmotic pressures of protein solutions.

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