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Analytical chromatography – the use of chromatography to determine the existence and possibly also the concentration of analyte(s) in a sample. Bonded phase – a stationary phase that is covalently bonded to the support particles or to the inside wall of the column tubing. Chromatogram – the visual output of the chromatograph. In the case ...
Affinity chromatography can be used in a number of applications, including nucleic acid purification, protein purification [9] from cell free extracts, and purification from blood. By using affinity chromatography, one can separate proteins that bind to a certain fragment from proteins that do not bind that specific fragment. [10]
Ion exchange chromatography is a very powerful tool for use in protein purification and is frequently used in both analytical and preparative separations. It is especially useful when purifying nucleic-acid binding proteins, where separation of the protein from the bound nucleic acid is required to obtain a pure sample devoid of nucleic acids ...
Chromatography is a physical method of separation that distributes the components you want to separate between two phases, one stationary (stationary phase), the other (the mobile phase) moving in a definite direction. Cold ethanol precipitation, developed by Cohn in 1946, manipulates pH, ionic strength, ethanol concentration and temperature to ...
Ion chromatography (or ion-exchange chromatography) is a form of chromatography that separates ions and ionizable polar molecules based on their affinity to the ion exchanger. [1] It works on almost any kind of charged molecule —including small inorganic anions, [ 2 ] large proteins , [ 3 ] small nucleotides , [ 4 ] and amino acids .
Size-exclusion chromatography, also known as molecular sieve chromatography, [1] is a chromatographic method in which molecules in solution are separated by their shape, and in some cases size. [2] It is usually applied to large molecules or macromolecular complexes such as proteins and industrial polymers . [ 3 ]
The use of displacement chromatography is rather limited, and is mostly used for preparative chromatography. The basic principle is based on a molecule with a high affinity for the chromatography matrix (the displacer) which is used to compete effectively for binding sites, and thus displace all molecules with lesser affinities. [ 28 ]
Fast protein liquid chromatography (FPLC) is a form of liquid chromatography that is often used to analyze or purify mixtures of proteins. As in other forms of chromatography, separation is possible because the different components of a mixture have different affinities for two materials, a moving fluid (the mobile phase) and a porous solid (the stationary phase).