Avidin column as a highly efficient and stable alternative for immobilization of ligands for affinity chromatography

✍ Scribed by Edward A. Bayer; Meir Wilchek

• Publisher: John Wiley and Sons
• Year: 1990
• Tongue: English
• Weight: 620 KB
• Volume: 3
• Category: Article
• ISSN: 0952-3499
• DOI: 10.1002/jmr.300030303

✦ Synopsis

Abstract

The avidin/biotin system was applied as a general mediator in the adsorption/desorption or immobilization of biologically active macromolecules to solid supports. In this context, model biotinylated proteins (lectins and antibodies) were attached to avidin‐coupled Sepharose. As examples for affinity chromatography, peanut agglutinin and anti‐transferrin antibody were used to isolate asialofetuin and transferrin, respectively. The capacity and product yields were significantly better than those achieved with conventional affinity chromatography on CNBr‐activated Sepharose columns containing the same lectin or antibody. Moreover, the columns were characterized by improved stability properties exhibiting remarkably low levels of leakage.