The Molecular Basis of Self-Association of Antibodies to IgG (Rheumatoid Factors) in Rheumatoid Arthritis
- 1 February 1974
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 71 (2), 517-521
- https://doi.org/10.1073/pnas.71.2.517
Abstract
The serum and synovial fluid of many patients with rheumatoid arthritis contain immune complexes composed of immunoglobulin G (IgG). In this study such complexes from one patient are shown to be formed by self-association of IgG-antibodies to IgG (IgG-rheumatoid factors), so that each molecule serves as an antibody as well as an antigen. All F(ab')(2) and Fab' fragments derived from these complexes have antibody binding sites for normal IgG. Due to a high association constant in the formation of a cyclic complex by these antibodies, normal IgG is excluded as an antigen. These studies serve as a model for further elucidation of presence of similar immune complexes in the serum and synovial fluid of patients with rheumatoid arthritis.Keywords
This publication has 22 references indexed in Scilit:
- Molecular composition and sedimentation characteristics of soluble antigen-antibody complexesBiochemistry, 1972
- Complement‐Fixing Intracellular Complexes of IgG Rheumatoid Factor in Rheumatoid Plasma Cells.Scandinavian Journal of Immunology, 1972
- The influence of polyvalency on the binding properties of antibodiesImmunochemistry, 1972
- Ultracentrifuge study of the self-association of fraction II of procarboxypeptidase ABiochemistry, 1970
- Hybrid formation of carboxypeptidase A and fraction II of procarboxypeptidase ABiochemistry, 1970
- SEDIMENTATION EQUILIBRIUM OF LOW‐MOLECULARWEIGHT ASSOCIATING SOLUTESAnnals of the New York Academy of Sciences, 1969
- Human monoclonal γG-cryoglobulins with anti—γ-globulin activityJCI Insight, 1968
- Characterization of the gamma-globulin complexes present in certain sera having high titers of anti-gamma-globulin activity.JCI Insight, 1966
- GAMMA GLOBULIN COMPLEXES IN RHEUMATOID ARTHRITIS AND CERTAIN OTHER CONDITIONSJCI Insight, 1961
- Separation of univalent fragments from the bivalent rabbit antibody molecule by reduction of disulfide bondsArchives of Biochemistry and Biophysics, 1960