Improvement of the performance of an immunoaffinity extraction method via region-specific immobilization of IgG

Using papaverine as a model target, an immunoaffinity column of high selectivity and binding capacity was prepared by utilizing covalent linkage between the Fc portion of IgG and the surface of Sepharose 4B support. Compared with the commonly used random coupling method, the binding capacity of the region-specific immobilized antibodies was increased from 0.04 to 0.2 mol of antigens/mol of antibodies and a much larger concentration factor was thus achieved. The obtained immunoaffinity column has been successfully used in pretreatment of pericarpium papaveris samples. The method offers an improved approach to immunoaffinity extraction that should be useful for purification and concentration of other targeted compounds in highly complex mixture.