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Improved removal of anti-A and anti-B antibodies from plasma using blood-group-active haptens
L Blomberg1, T Bratt, M A Chester
1BioCarb Technology AB, University Hospital, Lund, Sweden.
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.
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.