sepharose and Nasopharyngeal-Neoplasms

Con 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 IgG 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. By contrast IgG containing immune complexes in chronic hepatitis B seem to lack affinity for Con A-Sepharose.

Topics: Antigen-Antibody Complex; Burkitt Lymphoma; Chromatography, Affinity; Chronic Disease; Concanavalin A; Hepatitis B; Humans; Immune Sera; Immunoglobulin G; Nasopharyngeal Neoplasms; Sepharose

Sera of individuals with Burkitt's lymphoma and nasopharyngeal carcinoma, tested by consumption of hemolytic complement, were found by comparison with healthy individuals to have significantly increased levels of circulating immune complexes. The identity of the immune complexes was established by sucrose density gradient ultracentrifugation, which showed them to sediment between 10 and 19S. As they were adsorbable by rheumatoid factor--Sepharose 4B conjugates, it appeared that these complexes were composed of IgG. The complexes were retained by Concanavalin A--Sepharose columns and eluted by alpha methyl-D-mannoside, suggesting by analogy with model complexes that the antigens might be glycoproteins.

Topics: Adsorption; Antibodies, Heterophile; Antigen-Antibody Complex; Antigens, Heterophile; Burkitt Lymphoma; Cell Line; Centrifugation, Density Gradient; Chromatography, Affinity; Complement C3; Complement System Proteins; Concanavalin A; Hemolytic Plaque Technique; Humans; Immunoglobulin G; Male; Nasopharyngeal Neoplasms; Rheumatoid Factor; Sepharose