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Interaction between rabbit IgG immune complexes and Ricinus agglutinin
Ricinus communis agglutinin covalently bound to Sepharose 4B (RcA-Sepharose 4B) was able to selectively bind immune complexes consisting of antigen (bovine serum albumin) and rabbit IgG antibody which were rich in antibody (i.e., high molecular weight complexes of approximately 2000 000). No interaction was recorded between RcA-Sepharose 4B and immune complexes consisting of the antigen plus rabbit IgG antibody which were rich in antigen (i.e., complexes with a molecular weight of 300 000-500 000). These results indicate that binding to RcA is due to the increased density of galactose residues in the high molecular weight polymeric antibody component of the soluble immune complexes.
Ricinus communis agglutinin covalently bound to Sepharose 4B (RcA-Sepharose 4B) was able to selectively bind immune complexes consisting of antigen (bovine serum albumin) and rabbit IgG antibody which were rich in antibody (i.e., high molecular weight complexes of approximately 2000 000). No interaction was recorded between RcA-Sepharose 4B and immune complexes consisting of the antigen plus rabbit IgG antibody which were rich in antigen (i.e., complexes with a molecular weight of 300 000-500 000). These results indicate that binding to RcA is due to the increased density of galactose residues in the high molecular weight polymeric antibody component of the soluble immune complexes.