A new complement function: solubilization of antigen-antibody aggregates. | Zendy

Gary W. Miller | Zendy; Victor Nussenzweig | Zendy

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A new complement function: solubilization of antigen-antibody aggregates.

Author(s) -

Gary W. Miller,

Victor Nussenzweig

Publication year - 1975

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.72.2.418

Subject(s) - antibody , antigen , complement system , properdin , solubilization , antigen antibody complex , immune system , chemistry , epitope , biochemistry , biology , microbiology and biotechnology , immunology

Antigen-antibody aggregates are solubilized when incubated with fresh serum at 37 degrees, yielding immune-complexes of relatively small molecular weight which contain antigen, antibody, and complement (C3)determinants. Solubilization is complement-dependent,requires free Mg++ but not Ca++, and proceeds in sera from C4- or C5-deficient animals. It is accelerated in the presence of Ca++ in normal or C4-deficient guinea pig serum, suggesting involvement of the Cl-bypass activation of the properdin system. Immune precipitates can also be solubilized by monovalent fragments (Fab) of antibodies directed against determinants of the antibody molecules included in the antigen-antibody lattice. Similarly, it is suggested that complement-mediated solubilization might be induced by the combination of a complement fragment with the antibody in the immune-aggregate.

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