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  2. Affinity chromatography - Wikipedia

    en.wikipedia.org/wiki/Affinity_chromatography

    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]

  3. Fast protein liquid chromatography - Wikipedia

    en.wikipedia.org/wiki/Fast_protein_liquid...

    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).

  4. Expanded bed adsorption - Wikipedia

    en.wikipedia.org/wiki/Expanded_bed_adsorption

    The protein binding principles in EBA are the same as in classical column chromatography and the common ion-exchange, hydrophobic interaction and affinity chromatography ligands can be used. [1] After the adsorption step is complete, the fluidized bed is washed to flush out any remaining particulates.

  5. Chromatography - Wikipedia

    en.wikipedia.org/wiki/Chromatography

    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 ...

  6. Electrochromatography - Wikipedia

    en.wikipedia.org/wiki/Electrochromatography

    Electrochromatography is a chemical separation technique in analytical chemistry, biochemistry and molecular biology used to resolve and separate mostly large biomolecules such as proteins. It is a combination of size exclusion chromatography (gel filtration chromatography) and gel electrophoresis. These separation mechanisms operate ...

  7. Size-exclusion chromatography - Wikipedia

    en.wikipedia.org/wiki/Size-exclusion_chromatography

    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 ]

  8. Protein purification - Wikipedia

    en.wikipedia.org/wiki/Protein_purification

    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]

  9. Gel electrophoresis of proteins - Wikipedia

    en.wikipedia.org/.../Gel_electrophoresis_of_proteins

    Proteins separated by SDS-PAGE, Coomassie brilliant blue staining. Protein electrophoresis is a method for analysing the proteins in a fluid or an extract. The electrophoresis may be performed with a small volume of sample in a number of alternative ways with or without a supporting medium, namely agarose or polyacrylamide.