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Chromatography, pronounced / ˌ k r oʊ m ə ˈ t ɒ ɡ r ə f i /, is derived from Greek χρῶμα chrōma, which means "color", and γράφειν gráphein, which means "to write".". The combination of these two terms was directly inherited from the invention of the technique first used to separate biological pigme
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 ...
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 .
Compared with the Cohn process, the albumin purity went up from about 95% to 98% using chromatography, and the yield increased from about 65% to 85%. Small percentage increases make a difference in regard to sensitive measurements like purity. There is one big drawback in using chromatography, which has to do with the economics of the process.
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
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 ]