STUDIES ON HUMAN ANTIBODIES

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Abstract
Insoluble blood group substances prepared by copolymerization of soluble blood group substances with N-carboxy-L-leucine anhydride were used to absorb blood group antibodies from two human, high-titered anti-A sera. After the absorbants were washed free of nonspecific serum proteins, blood group antibodies were eluted either with pH 3.62 acetate buffer, or at neutral pH with monosaccharide haptens of the A or B antigenic determinants (N-acetyl-D-galactosamine or D-galactose respectively). The purified anti-A antibodies were characterized, immunoelectrophoretically, as γM-, γA-, and γG-immunoglobulins. These were further separated into γM- and γG-fractions by gel filtration or density gradient centrifugation. Both γM- and one of the two γG-antibody fractions contained K and L light chain determinants; the remaining γG-fraction was comprised, almost totally, of type K molecules.