Interaction between soluble immune complexes and glass-fiber filters.
The two components of soluble antigen--antibody complexes, at the antigen excess, exhibit an increase in their binding ability to glass-fiber filters. This is demonstrated in two systems. In the 125I-BSA--anti-BSA system the proportion of 125I-BSA bound to the filter is markedly increased in the presence of anti-BSA antibodies. More than 80% of the antibody bound BSA can be removed by passage through the filter. In the other system, mouse gamma globulin (MGG)--125I-anti-MGG, the proportion of antibody bound to the filter increases with the increase in antigen concentration, whilst the presence of another, non-related, gamma globulin has little effect on the binding. The possible mechanisms for the binding of soluble complexes to the glass fibers are suggested and discussed.
D000818:Animals; D000936:Antigen-Antibody Complex; D001666:Binding Sites, Antibody; D005374:Filtration / Q000295:instrumentation*; D005898:Glass; D006801:Humans; D007457:Iodine Radioisotopes; D051379:Mice; D011817:Rabbits; D012710:Serum Albumin, Bovine / Q000276:immunology; D012995:Solubility; D005719:gamma-Globulins / Q000276:immunology
D000936:Antigen-Antibody Complex; D007457:Iodine Radioisotopes; D005719:gamma-Globulins; D012710:Serum Albumin, Bovine