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The protein manufacturing cost remains high and there is a growing demand to develop cost efficient and rapid protein purification methods. Understanding the different protein purification methods and optimizing the downstream processing is critical to minimize production costs while maintaining the quality of acceptable standards of homogeneity. [2]
Proteins of the erythrocyte membrane separated by SDS-PAGE according to their molecular masses. SDS-PAGE (sodium dodecyl sulfate–polyacrylamide gel electrophoresis) is a discontinuous electrophoretic system developed by Ulrich K. Laemmli which is commonly used as a method to separate proteins with molecular masses between 5 and 250 kDa.
Ammonium sulfate is an inorganic salt with a high solubility that disassociates into ammonium (NH + 4) and sulfate (SO 2− 4) in aqueous solutions. [1] Ammonium sulfate is especially useful as a precipitant because it is highly soluble, stabilizes protein structure, has a relatively low density, is readily available, and is relatively inexpensive.
Protein precipitation is widely used in downstream processing of biological products in order to concentrate proteins and purify them from various contaminants. For example, in the biotechnology industry protein precipitation is used to eliminate contaminants commonly contained in blood. [1]
Protein electrophoresis is a method for analysing the proteins in a fluid or an extract. The electrophoresis may be performed with a small volume of sample in a number of alternative ways with or without a supporting medium, namely agarose or polyacrylamide .
Pure results of a successful purification process are termed isolate. The following list of chemical purification methods should not be considered exhaustive. Affinity purification purifies proteins by retaining them on a column through their affinity to antibodies, enzymes, or receptors that have been immobilised on the column.