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Affinity chromatography is a method of separating a biomolecule from a mixture, ... Inorganic sources are moronic acid, metal chelates and triazine dyes. [7]
Dye-ligand affinity chromatography is one of the Affinity chromatography techniques used for protein purification of a complex mixture. Like general chromatography, but using dyes to apply on a support matrix of a column as the stationary phase that will allow a range of proteins with similar active sites to bind to, refers to as pseudo-affinity.
The biotin tag can be used in affinity chromatography together with a column that has avidin (or streptavidin or neutravidin) bound to it, which is the natural ligand for biotin. However, harsh conditions (e.g., 6M GuHCl at pH 1.5) are needed to break the avidin/streptavidin - biotin interaction, which will most likely denature the protein ...
Periodic counter-current chromatography (PCC) is a method for running affinity chromatography in a quasi-continuous manner. Today, the process is mainly employed for the purification of antibodies in the biopharmaceutical industry [1] as well as in research and development. When purifying antibodies, protein A is used as affinity matrix ...
The Strep-tag system is a method which allows the purification and detection of proteins by affinity chromatography.The Strep-tag II is a synthetic peptide consisting of eight amino acids (Trp-Ser-His-Pro-Gln-Phe-Glu-Lys).
Proteins can coordinate metal ions on their surface and it is possible to separate proteins using chromatography by making use of the difference in their affinity to metal ions. This is termed as immobilized metal ion affinity chromatography (IMAC), as originally introduced in 1975 under the name metal chelate affinity chromatography. [3]
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