title: Protein A, hydroxyapatite and diethylaminoethyl: evaluation of three procedures for the preparative purification of monoclonal antibodies by high-performance liquid chromatography.
abstract: Three rapid, reproducible and feasible monoclonal antibody purification procedures by means of high-performance liquid chromatography have been evaluated. The stationary phases employed were high-performance hydroxyapatite, high-performance Protein A and high-performance anion-exchange resin. The purity of the final immunoglobulin preparations was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions and, subsequently, by high-performance gel permeation chromatography. The immunoreactivity of purified monoclonal antibodies was determined by the radioimmunoassay method.
authors.affiliation: Department of Clinical Chemistry and Propedeutic Biochemistry, University of Brescia, Italy.
authors.forename: C
authors.initials: C
authors.lastname: Poiesi
authors.forename: A
authors.initials: A
authors.lastname: Tamanini
authors.forename: S
authors.initials: S
authors.lastname: Ghielmi
authors.forename: A
authors.initials: A
authors.lastname: Albertini
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal / Q000302:isolation & purification*; D002848:Chromatography, DEAE-Cellulose; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006882:Hydroxyapatites; D051379:Mice; D013205:Staphylococcal Protein A
chemical_list: D000911:Antibodies, Monoclonal; D006882:Hydroxyapatites; D013205:Staphylococcal Protein A