Efficient recovery of recombinant proteins using membrane-based immunoaffinity chromatography (MIC)

✍ Scribed by Michele Nachman; Abdul R. M. Azad; Pascal Bailon

• Publisher: John Wiley and Sons
• Year: 1992
• Tongue: English
• Weight: 804 KB
• Volume: 40
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/bit.260400503

✦ Synopsis

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-a2a 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-a 2a, interleukin-2, and interleukin-2 receptor, have been puri- fied 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.