title: Efficient recovery of recombinant proteins using membrane-based immunoaffinity chromatography (MIC).
abstract: A systematic approach to the design and development of membrane-based immunoaffinity systems for the purification of recombinant proteins is presented. The preparation and characterization of immunoaffinity membranes are described. The immunoaffinity purification process for recombinant interferon-alpha2a is used as a model system to determine the operational parameters in membrane-based immunoaffinity chromatography. The high volumetric throughput of membranes, combined with the typically fastbinding kinetics of antigen-antibody interactions, enable the purification of recombinant proteins from dilute feed stream in less time, using less antibody than conventional systems. Three recombinant proteins, human interferon-alpha2a, interleukin-2, and interleukin-2 receptor, have been purified efficiently employing membrane-based immunoaffinity chromatography. Overall, membrane-based immunoaffinity chromatography is shown to be a viable and scalable method, ideal for the industrial-scale production of recombinant proteins.
authors.affiliation: Department of Protein Biochemistry, Roche Research Center, Hoffmann-La Roche, Inc., Nutley, New Jersey 07110, USA.
authors.forename: M
authors.initials: M
authors.lastname: Nachman
authors.forename: A R
authors.initials: AR
authors.lastname: Azad
authors.forename: P
authors.initials: P
authors.lastname: Bailon