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Ammonium sulfate is an inorganic salt with a high solubility that disassociates into ammonium (NH + 4) and sulfate (SO 2− 4) in aqueous solutions. [1] Ammonium sulfate is especially useful as a precipitant because it is highly soluble, stabilizes protein structure, has a relatively low density, is readily available, and is relatively inexpensive.
Ammonium sulfate precipitation is a common method for protein purification by precipitation. As the ionic strength of a solution increases, the solubility of proteins in that solution decreases. Being extremely soluble in water, ammonium sulfate can "salt out" (precipitate) proteins from aqueous solutions.
Salting out (also known as salt-induced precipitation, salt fractionation, anti-solvent crystallization, precipitation crystallization, or drowning out) [1] is a purification technique that utilizes the reduced solubility of certain molecules in a solution of very high ionic strength.
The following chart shows the solubility of various ionic compounds in water at 1 atm pressure and room temperature (approx. 25 °C, 298.15 K). "Soluble" means the ionic compound doesn't precipitate, while "slightly soluble" and "insoluble" mean that a solid will precipitate; "slightly soluble" compounds like calcium sulfate may require heat to precipitate.
The precipitation method is the one used for the determination of the amount of calcium in water. Using this method, an excess of oxalic acid, H 2 C 2 O 4, is added to a measured, known volume of water. By adding a reagent, here ammonium oxalate, the calcium will precipitate as calcium oxalate. The proper reagent, when added to aqueous solution ...
This can be due to temperature changes, solvent evaporation, or by mixing solvents. Precipitation occurs more rapidly from a strongly supersaturated solution. The formation of a precipitate can be caused by a chemical reaction. When a barium chloride solution reacts with sulphuric acid, a white precipitate of barium sulphate is formed.
During the ammonium sulfate precipitation step, hydrophobic groups present on the proteins are exposed to the atmosphere, attracting other hydrophobic groups; the result is formation of an aggregate of hydrophobic components. In this case, the protein precipitate will typically be visible to the naked eye. One advantage of this method is that ...
By contrast, later salts in the series increase the solubility of nonpolar molecules ("salting in") and decrease the order in water; in effect, they weaken the hydrophobic effect. [14] [15] The "salting out" effect is commonly exploited in protein purification through the use of ammonium sulfate precipitation. [16]