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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 ...
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 ...
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).
Some techniques commonly used in bioanalytical studies include: Hyphenated techniques. LC–MS (liquid chromatography–mass spectrometry) GC–MS (gas chromatography–mass spectrometry) LC–DAD (liquid chromatography–diode array detection) CE–MS (capillary electrophoresis–mass spectrometry) Chromatographic methods
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 .
A myc tag is a polypeptide protein tag derived from the c-myc gene product that can be added to a protein using recombinant DNA technology. It can be used for affinity chromatography, then used to separate recombinant, overexpressed protein from wild type protein expressed by the host organism.
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]
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 ]