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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.
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.