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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.
Being extremely soluble in water, ammonium sulfate can "salt out" (precipitate) proteins from aqueous solutions. [3] [4] Precipitation by ammonium sulfate is a result of a reduction in solubility rather than protein denaturation, thus the precipitated protein can be resolubilized through the use of standard buffers. [5]
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.
In an aqueous solution, precipitation is the "sedimentation of a solid material (a precipitate) from a liquid solution". [ 1 ] [ 2 ] The solid formed is called the precipitate . [ 3 ] In case of an inorganic chemical reaction leading to precipitation, the chemical reagent causing the solid to form is called the precipitant .
The tables below provides information on the variation of solubility of different substances (mostly inorganic compounds) in water with temperature, at one atmosphere pressure.
Glauber's salt – sodium sulfate. Na 2 SO 4; Sal alembroth – salt composed of chlorides of ammonium and mercury. Sal ammoniac – ammonium chloride. Sal petrae (Med. Latin: "stone salt")/salt of petra/saltpetre/nitrate of potash – potassium nitrate, KNO 3, typically mined from covered dungheaps.
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The "salting out" effect is commonly exploited in protein purification through the use of ammonium sulfate precipitation. [16] However, these salts also interact directly with proteins (which are charged and have strong dipole moments) and may even bind specifically (e.g., phosphate and sulfate binding to ribonuclease A).