ABSTRACT
This chapter presents a general overview of the principles of chromatography and electrophoresis, as used in protein biotechnology. The ability of a chromatographic media to separate the components of sample mixture is controlled by the distribution of the components between a solid stationary phase and a liquid mobile phase. In adsorption or normal-phase chromatography, binding to the stationary phase is due to polar interactions, especially hydrogen bonding. Size exclusion chromatography or gel permeation chromatography columns contain porous particles with a selected range of pore diameters. Affinity chromatography takes advantage of the specific and selective binding between two biomolecules. Electrophoresis can be a complementary technique to chromatography. Electrophoresis refers to the migration of sample components in an electric field. Paper electrophoresis involves the use of thin strips of cellulose or cellulose acetate as the matrix. The most popular mode of electrophoresis for proteins is polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate.
