Abstract
Con A[concanavalin A]-Sepharose affinity chromatography may be used in the analysis and classification of immune complexes. Experiments with model immune complexes suggest that the degree of affinity of an immune complex for Con A-Sepharose is determined by the antigen rather than the Ig[immunoglobulin]G antibody of the complex. It is possible that partial characterization of unknown antigens linked to IgG in immune complexes may be achieved in many diseases. Preliminary explorations with selected human sera indicate that the IgG containing immune complexes in Burkitt''s lymphoma and nasopharyngeal carcinoma have affinity for Con A-Sepharose. IgG containing immune complexes in chronic hepatitis B seem to lack affinity for Con A-Sepharose.