2004
DOI: 10.1021/cr030454p
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Critical Appraisal of Salting-Out and Its Implications for Chemical and Biological Sciences

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Cited by 173 publications
(151 citation statements)
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“…The temperature must be kept low to avoid denaturation of the proteins. Mechanistically, organic solvents reduce the proteins' solubility by decreasing the medium's dielectric constant (12). The stability of proteins' native structures in water-cosolvent mixtures has been examined in the context of enzyme catalysis in "good and bad solvents" (13).…”
Section: Protein Purificationmentioning
confidence: 99%
“…The temperature must be kept low to avoid denaturation of the proteins. Mechanistically, organic solvents reduce the proteins' solubility by decreasing the medium's dielectric constant (12). The stability of proteins' native structures in water-cosolvent mixtures has been examined in the context of enzyme catalysis in "good and bad solvents" (13).…”
Section: Protein Purificationmentioning
confidence: 99%
“…When surfactant and salt are mixed in solution, salting-out phenomenon often happens [15][16][17][18]. According to hydration theory [19] salting-out is the result of preferential movement of water molecules, which immobilize and quench their role as solvents, from coordination shells of surfactant molecules to those of salts. The effects of halide salts on the growth of micelles in ionic surfactant solutions have been systematically studied [20][21].…”
Section: Resultsmentioning
confidence: 99%
“…According to hydration theory [10] salting-out is the result of preferential movement of water molecules, which immobilize and quench their role as solvents, from coordination shells of surfactant molecules to those of salts. The effects of halide salts on the growth of micelles in ionic surfactant solutions have been systematically studied [11,12].…”
Section: Resultsmentioning
confidence: 99%