Immunoaffinity CE for Proteomics Studies.

A living organism is a highly evolved system composed of many interwoven mo- lecular networks.These networks primarily involve proteins that enable and control virtually every cellular chemical process.They do this through a very large number of molecular interactions with other proteins, sugars, lipids, nucleic acids, and low-mass molecules, including enzyme-substrate interactions (1-6).A vast amount of information has accumulated on the chemical and physicochemical molecular interactions involved in the specific affinity of an antibody-antigen interaction, as well as for other related affinity associations among a wide range of substances (7-13).The high selectivities and affinities of antibody-antigen interactions make them among the most finely tuned noncovalent bonds exhibited by proteins.Biospecific molecular interactions among a large number of substances have been used extensively for designing affinity chromatographic purifications for a wide range of low-mass molecules and larger biomolecules (8-13).Most of these interactions between a ligand and its corresponding receptor occur when one of the affinity partners is immobilized.Under such conditions, the properties of the interaction(s) differ from those exhibited by a similar system in free solution (14).Therefore, solid-phase purification is a constant challenge for the user, and almost every step of the association and dissociation processes must be optimized and validated for maximum performance (14 -16).Although thousands of substances have been purified using affinity chromatography, the This 2-D separation technique can complement MS-based proteomics methods.