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Before a specific protein can be identified and its properties can be studied, the protein must usually be separated from a sample of plant or animal tissue or extracted from a complex mixture. Extraction and purification are vital components of almost any protein-specific research effort. But the methods used during these processes will depend on the nature of both the protein and the solution. Sometimes the specific protein is caught in a matrix of other protein molecules, and sometimes it’s surrounded by non-protein biological elements. In either case, a small sample of the protein may be need for research and analytical purposes, or a large quantity of the purified protein may be necessary for industrial or commercial reasons. Protein purification is a series of processes intended to isolate a single type of protein from a complex mixture. Protein purification is vital for the characterization of the function, structure and interactions of the protein of interest. The starting material is usually a biological tissue or a microbial culture. The various steps in the purification process may free the protein from a matrix that confines it, separate the protein and non-protein parts of the mixture, and finally separate the desired protein from all other proteins. Separation of one protein from all others is typically the most laborious aspect of protein purification. Separation steps may exploit differences in (for example) protein size, physico-chemical properties, binding affinity and biological activity. Biodetergents such as Triton-X, n-Octyl-β-D-Glucopyranoside, and CHAPS are commonly used for solubilizing, extracting, and purifying membrane proteins.
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