Application Note: Higher Efficiency Protein Purification with Ion Exchange Tips - METTLER TOLEDO
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Application Note: Higher Efficiency Protein Purification with Ion Exchange Tips

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Separation of Bovine Serum Albumin and Chicken Egg Lysozyme using PureSpeed Ion Exchange Tips.

Protein purification is carried out extensively in chemical and biological research. In order to study a given protein, or use it for medicinal or biotechnological purposes, it must be separated from the cellular or chemical mixture initially used to produce it. Ion exchange chromatography is widely used for protein purification. In this technique, a resin with positively or negatively charged moieties appended on its surface is used to resolve proteins with different net positive or negative charges at a defined pH.

After binding different proteins to an ion exchange resin, a salt or pH gradient is used to elute individual protein species. The salt concentration or pH required for the elution of a particular protein depends on the interaction strength between the protein and the resin. For cation exchange chromatography, proteins with a higher net positive charge interact more strongly with the resin and require more salt or higher pH in the elution media to be removed from the resin.

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