In ion exchange chromatography, the net charge and the charge distribution on the surface of a protein determine the interaction of the protein with the charged groups on the surface of the packing material. The surface charges of protein and packing material must be opposite, so that an interaction can take place. The modification of different parameters, such as the pH value of the buffer, the buffer composition, the gradient of the gradient, and the salt with which the gradient is built, enable a wide range of possibilities for optimizing a successful separation. At each pH, a protein has a positive or negative net charge due to the charge state of the amino acids. Accordingly, this protein, if positively charged, will bind either to negatively charged materials or otherwise to positively charged materials. The separation takes place essentially according to charge and size of the ions. As materials for the gel matrix, resins such as polystyrene, cellulose, and crosslinked polyacrylamide or polydextran gels are used. It is distinguished by strong and weak anion or cation exchangers. Ion exchange chromatography is normally performed at pH values which leave the protein in its active conformation.
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