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In chemistry, the common-ion effect refers to the decrease in solubility of an ionic precipitate by the addition to the solution of a soluble compound with an ion in common with the precipitate. [1] This behaviour is a consequence of Le Chatelier's principle for the equilibrium reaction of the ionic association / dissociation .
In chemistry, Le Chatelier's principle (pronounced UK: / l ə ʃ æ ˈ t ɛ l j eɪ / or US: / ˈ ʃ ɑː t əl j eɪ /) [1] is a principle used to predict the effect of a change in conditions on chemical equilibrium. [2] Other names include Chatelier's principle, Braun–Le Chatelier principle, Le Chatelier–Braun principle or the equilibrium ...
The common-ion effect is the effect of decreased solubility of one salt when another salt that has an ion in common with it is also present. For example, the solubility of silver chloride, AgCl, is lowered when sodium chloride, a source of the common ion chloride, is added to a suspension of AgCl in water. [5]
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Henry Louis Le Chatelier [1] (French pronunciation: [ɑ̃ʁi lwi lə ʃɑtəlje]; 8 October 1850 – 17 September 1936) was a French chemist of the late 19th and early 20th centuries. He devised Le Chatelier's principle , used by chemists and chemical engineers to predict the effect a changing condition has on a system in chemical equilibrium .
However, a "salting in" effect has also been observed, for example for the effective Henry's law constant of glyoxal. The effect can be described with the Sechenov equation, named after the Russian physiologist Ivan Sechenov (sometimes the German transliteration "Setschenow" of the Cyrillic name Се́ченов is used). There are many ...
Sometimes Lüders band transition into the Portevin–Le Chatelier effect while changing the temperature or strain rate, this implies these are related phenomena [4] Lüders bands are known as a strain softening instability. [5]
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 ).