title: Dissociation and fractionation of heavy and light chains from IgG monoclonal antibodies.
abstract: A basic method for dissociation and fractionation of monoclonal IgG heavy and light chain is described. It employs less noxious and hazardous reagents than the classical mercaptoethanol/propionic acid process and replaces size exclusion chromatography with cation exchange on a monolith to improve productivity. Significant scope remains to refine the conditions. The method can be applied to other disulfide bonded proteins with significant affinity for cation exchangers.
authors.affiliation: Bioprocessing Technology Institute, 20 Biopolis Way, Centros, Singapore. pete_gagnon@mac.com
authors.forename: Pete
authors.initials: P
authors.lastname: Gagnon
authors.forename: George
authors.initials: G
authors.lastname: Rodriquez
authors.forename: Simin
authors.initials: S
authors.lastname: Zaidi
mesh_terms: D000911:Antibodies, Monoclonal / Q000737:chemistry*; D002412:Cations / Q000737:chemistry; D002852:Chromatography, Ion Exchange / Q000379:methods*; D007074:Immunoglobulin G / Q000737:chemistry*; D007143:Immunoglobulin Heavy Chains / Q000737:chemistry / Q000302:isolation & purification*; D007147:Immunoglobulin Light Chains / Q000737:chemistry / Q000302:isolation & purification*; D014508:Urea / Q000737:chemistry; D014783:Viscosity
chemical_list: D000911:Antibodies, Monoclonal; D002412:Cations; D007074:Immunoglobulin G; D007143:Immunoglobulin Heavy Chains; D007147:Immunoglobulin Light Chains; D014508:Urea