Quantitative analyses of complement fixation in three immune complex systems.
The quantitative interaction of three different immune complex systems with complement has been investigated. dsDNA/anti-DNA, heat-aggregated IgG subfractions, and human IgG/rabbit anti-human IgG complexes were tested for their ability to consume complement (immune haemolysis assay) and to bind to red blood cells in a complement-mediated reaction (the RBC-CF assay). Our results indicate that some physical and immunological properties of the dsDNA/anti-DNA immune complex systems are significantly different from those of immune complexes that involve more common globular protein antigens. This difference in properties may help explain the role of dsDNA/anti-DNA immune complexes in systemic lupus erythematosus pathogenesis.
D000818:Animals; D000974:Antibodies, Antinuclear / Q000276:immunology; D000936:Antigen-Antibody Complex / Q000378:metabolism*; D003168:Complement Fixation Tests / Q000379:methods; D003165:Complement System Proteins / Q000378:metabolism*; D004306:Dose-Response Relationship, Immunologic; D006358:Hot Temperature; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism; D011489:Protein Denaturation; D011817:Rabbits; D012995:Solubility
D000974:Antibodies, Antinuclear; D000936:Antigen-Antibody Complex; D007074:Immunoglobulin G; D003165:Complement System Proteins