Protein purification and separation is done by all Except
Highly purified protein is essential for the detailed examination of its physical and functional propeies. It may require the successive application of multiple purification techniques. Selective precipitation exploits differences in relative solubility of individual proteins as a function of pH (isoelectric precipitation), polarity (precipitation with ethanol or acetone), or salt concentration (salting out with ammonium sulfate). Chromatographic techniques separate one protein from another based upon the difference in their size (size exclusion chromatography), charge (ion-exchange chromatography), hydrophobicity (hydrophobic interaction chromatography), or ability to bind a specific ligand (affinity chromatography).The most widely used method for determining the purity of a protein is SDS-PAGE--polyacrylamide gel electrophoresis (PAGE) in the presence of the anionic detergent sodium dodecyl sulfate (SDS).Densitometry is a method to quantify the proteinsRef: Harper; 30th edition; Pg: 26
Chromatography
Precipitation
Electrophoresis
Densitometry
Structure and function of protein