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Protein precipitation is widely used in downstream processing of biological products in order to concentrate proteins and purify them from various contaminants. For example, in the biotechnology industry protein precipitation is used to eliminate contaminants commonly contained in blood. [ 1 ]
Unwanted proteins can be removed from a protein solution mixture by salting out as long as the solubility of the protein in various concentrations of salt solution is known. After removing the precipitate by filtration or centrifugation , the desired protein can be precipitated by altering the salt concentration to the level at which the ...
RNA partitions in the aqueous phase, while proteins and DNA partition into the organic/interphase (left). The RNA is then precipitated in an alcohol (right). Acid guanidinium thiocyanate-phenol-chloroform extraction (abbreviated AGPC) is a liquid–liquid extraction technique in biochemistry and molecular biology.
Phosphotungstic acid (PTA) or tungstophosphoric acid (TPA), is a heteropoly acid with the chemical formula H 3 P W 12 O 40]. It forms hydrates H 3 [PW 12 O 40]·nH 2 O. It is normally isolated as the n = 24 hydrate but can be desiccated to the hexahydrate (n = 6). [2] EPTA is the name of ethanolic phosphotungstic acid, its alcohol solution used ...
Millon's reagent is an analytical reagent used to detect the presence of soluble proteins. A few drops of the reagent are added to the test solution, which is then heated gently. A reddish-brown coloration or precipitate indicates the presence of tyrosine residue which occur in nearly all proteins. [1]
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. [4]
Concentrated nitric acid is added to a protein solution from the side of the test tube to form two layers. A white ring appears between the two layers if the test is positive. [1] Heller's test is commonly used to test for the presence of proteins in urine. [2] This test was discovered by the Austrian Chemist, Johann Florian Heller (1813-1871).
Folin reagent is stable at only acidic conditions and the method is susceptible to skewing results depending on how much tryptophan and tyrosine is present in the examined protein. [12] The Folin reagent binds to tryptophan and tyrosine which means the concentration of the two amino acids affects the sensitivity of the method.
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