Search results
Results from the WOW.Com Content Network
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.
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.
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.
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 ...
While precipitation reactions can be used for making pigments, removing ions from solution in water treatment, and in classical qualitative inorganic analysis, precipitation is also commonly used to isolate the products of an organic reaction during workup and purification operations. Ideally, the product of the reaction is insoluble in the ...
The ideal salt for protein precipitation is most effective for a particular amino acid composition, inexpensive, non-buffering, and non-polluting. The most commonly used salt is ammonium sulfate. There is a low variation in salting out over temperatures 0 °C to 30 °C.
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]