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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 .
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 ...
Desalting and buffer exchange are two of the most common gel filtration chromatography applications, and they can be performed using the same resin. Desalting and buffer exchange both entail recovering the components of a sample in whatever buffer is used to pre-equilibrate the small, porous polymer beads (resin).
Good's buffers (also Good buffers) are twenty buffering agents for biochemical and biological research selected and described by Norman Good and colleagues during 1966–1980. [ 1 ] [ 2 ] [ 3 ] Most of the buffers were new zwitterionic compounds prepared and tested by Good and coworkers for the first time, though some ( MES , ADA , BES , Bicine ...
Because there is a difference in concentration of ions on either side of the membrane, the pH (defined using the relative activity) may also differ when protons are involved [citation needed]. In many instances, from ultrafiltration of proteins to ion exchange chromatography, the pH of the buffer adjacent to the charged groups of the membrane ...
Dialysis is the process used to change the matrix of molecules in a sample by differentiating molecules by the classification of size. [6] [7] It relies on diffusion, which is the random, thermal movement of molecules in solution (Brownian motion) that leads to the net movement of molecules from an area of higher concentration to a lower concentration until equilibrium is reached.
Schematic structure of DEAE-C: positively charged diethylaminoethanol groups can bind negative ions. Diethylaminoethyl cellulose (DEAE-C) is a positively charged resin used in ion-exchange chromatography, a type of column chromatography, for the separation and purification of proteins and nucleic acids.
Elution principle of column chromatography. In analytical and organic chemistry, elution is the process of extracting one material from another by washing with a solvent: washing of loaded ion-exchange resins to remove captured ions, or eluting proteins or other biopolymers from a gel electrophoresis or chromatography column.