Purification of a monoclonal IgA with antiheparin activity

A monoclonal IgA with antiheparin activity was obtained from a hyperlipidemic plasma. For the separation of the IgA antibody the plasma was passed through a column of Bio-Gel P-6 to eliminate the unbound heparin. As a second step, intervent dilution chromatography was used. The active peak of the intervent dilution chromatography was finally purified on heparin coupled to epoxy-activated sepharose 6B at pH 4.0. The obtained fraction gave a single arc with sodium dodecyl sulfate polyacrylamide gel electrophoresis. Using a lower pH (pH 2.8) for the separation, an aggregation of the IgA molecule was observed. Either the monomere or the aggregated IgA had a strong antiheparin activity. The presence of this antiheparin antibody is suggesting the possibility that certain immunoglobulins may play a role as heparin inhibitors in the development of hyperlipidemias.