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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 ]
The protein of interest then reduces its surface area, which diminishes its contact with the solvent. This is shown by the folding and self-association, which ultimately leads to precipitation. The folding and self-association of the protein pushes out free water, leading to an increase in entropy and making this process energetically favorable ...
The protein manufacturing cost remains high and there is a growing demand to develop cost efficient and rapid protein purification methods. Understanding of the different protein purification methods and optimizing the downstream processing are critical to minimize production costs while maintaining the quality of acceptable standards of homogeneity. [2]
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 "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).
Immunoprecipitation of intact protein complexes (i.e. antigen along with any proteins or ligands that are bound to it) is known as co-immunoprecipitation (Co-IP). Co-IP works by selecting an antibody that targets a known protein that is believed to be a member of a larger complex of proteins.
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 ]
The study of protein folding began in 1910 with a famous paper by Harriette Chick and C. J. Martin, in which they showed that the flocculation of a protein was composed of two distinct processes: the precipitation of a protein from solution was preceded by another process called denaturation, in which the protein became much less soluble, lost ...