Abstract Precipitation experiments of electro-positive albumin by the action of a wide number of salts, and at different concentrations, were performed at a constant temperature (25 °C). The pH range studied… Click to show full abstract
Abstract Precipitation experiments of electro-positive albumin by the action of a wide number of salts, and at different concentrations, were performed at a constant temperature (25 °C). The pH range studied covered extreme acidic conditions up to hydronium concentrations where the dissociation of the protein carboxyl groups becomes noticeable. The time required for the clouding phenomenon to occur and the quantity of salted-out protein were also ascertained. The results here reported show that the salt anion is the main salting-out species for the positively charged protein, where their efficacy in salting-out albumin from aqueous solution increases in the order: F−
               
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