Abstract
Highly efficient anti-blood group A and B immunoadsorbents for extracorporeal treatment were developed by immobilizing A and B trisaccharide and A tetrasaccharide haptens on Sepharose 4FF and Fractogel TSK using three different methods. The adsorption of the IgG and IgM anti-A antibodies was essentially the same regardless of the A hapten used or the method of oligosaccharide coupling. The adsorption of IgM anti-A was found to be more sensitive than IgG anti-A to changes in column flow rate. The binding of both the IgM and IgG antibodies was slightly lower at 37 degrees C than at 22 degrees C. An anti-A/anti-B adsorbent column potentially suitable for treatment of patients was prepared. A column switching system resulted in a more efficient adsorption of antibodies. Hapten leakage from the column was very low. No nonspecific adsorption of plasma proteins to the column (other than traces of albumin) could be detected.
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