Abstract
The antigen dependency of Fc-mediated immune precipitation was investigated by comparing the immune precipitation of three different protein antigens (bovine serum albumin, BSA, human plasma transferrin, HPT, and human fibrinogen, HFg) using specific intact rabbit IgG antibodies and isomolar solutions of the corresponding F(ab')2 fragments. We found that this precipitin mechanism is highly antigen-dependent both quantitatively and qualitatively. Sucrose density gradient ultracentrifugation was used for the identification of Fc-precipitating immune complexes, and we demonstrated that different types of complexes take part in Fc-mediated immune precipitation in the different antigen-antibody systems. Thus, only small complexes are involved in the HFg system, whereas small as well as large complexes precipitate by this mechanism in the BSA and the HPT systems. The specificity of Fc-mediated immune precipitation was studied by mixing human serum albumin (HSA)-anti-HSA IgG complexes with either HPT-anti-HPT IgG or HFg-anti-HFg IgG complexes. These investigations show that Fc-mediated immune precipitation is a specific process due to the preferential binding of homologous complexes.
Full text
PDF











Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Arend W. P., Mannik M. Determination of soluble immune complex molar composition and antibody association constants by ammonium sulfate precipitation. J Immunol. 1974 Feb;112(2):451–461. [PubMed] [Google Scholar]
- CHARLWOOD P. A. ULTRACENTRIFUGAL CHARACTERISTICS OF HUMAN, MONEKY AND RAT TRANSFERRINS. Biochem J. 1963 Sep;88:394–398. doi: 10.1042/bj0880394. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DULBECCO R., VOGT M. Plaque formation and isolation of pure lines with poliomyelitis viruses. J Exp Med. 1954 Feb;99(2):167–182. doi: 10.1084/jem.99.2.167. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fowler W. E., Erickson H. P. Trinodular structure of fibrinogen. Confirmation by both shadowing and negative stain electron microscopy. J Mol Biol. 1979 Oct 25;134(2):241–249. doi: 10.1016/0022-2836(79)90034-2. [DOI] [PubMed] [Google Scholar]
- Fritz R. B., Lassiter S., Day E. D. The effect of iodination on antifibrinogen antibodies with respect to precipitating and adsorption activities. Immunochemistry. 1967 Sep;4(5):283–293. doi: 10.1016/0019-2791(67)90111-5. [DOI] [PubMed] [Google Scholar]
- HUNTER W. M., GREENWOOD F. C. Preparation of iodine-131 labelled human growth hormone of high specific activity. Nature. 1962 May 5;194:495–496. doi: 10.1038/194495a0. [DOI] [PubMed] [Google Scholar]
- Heidelberger M. QUANTITATIVE ABSOLUTE METHODS IN THE STUDY OF ANTIGEN-ANTIBODY REACTIONS. Bacteriol Rev. 1939 Jun;3(1):49–95. doi: 10.1128/br.3.1.49-95.1939. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kragh-Hansen U. Molecular aspects of ligand binding to serum albumin. Pharmacol Rev. 1981 Mar;33(1):17–53. [PubMed] [Google Scholar]
- Marrack J. R., Richards C. B. Light-scattering studies of the formation of aggregates in mixtures of antigen and antibody. Immunology. 1971 Jun;20(6):1019–1040. [PMC free article] [PubMed] [Google Scholar]
- Metzger H. The effect of antigen on antibodies: recent studies. Contemp Top Mol Immunol. 1978;7:119–152. doi: 10.1007/978-1-4757-0779-3_4. [DOI] [PubMed] [Google Scholar]
- Møller N. P., Christiansen G. Fc-mediated immune precipitation. III. Visualization by electron microscopy. Immunology. 1983 Mar;48(3):469–476. [PMC free article] [PubMed] [Google Scholar]
- Møller N. P. Fc-mediated immune precipitation. I. A new role of the Fc-portion of IgG. Immunology. 1979 Nov;38(3):631–640. [PMC free article] [PubMed] [Google Scholar]
- Møller N. P., Steensgaard J. Fc-mediated immune precipitation. II. Analysis of precipitating immune complexes by rate-zonal ultracentrifugation. Immunology. 1979 Nov;38(3):641–648. [PMC free article] [PubMed] [Google Scholar]
- NISONOFF A., WISSLER F. C., LIPMAN L. N., WOERNLEY D. L. Separation of univalent fragments from the bivalent rabbit antibody molecule by reduction of disulfide bonds. Arch Biochem Biophys. 1960 Aug;89:230–244. doi: 10.1016/0003-9861(60)90049-7. [DOI] [PubMed] [Google Scholar]
- Rodwell J. D., Lih-Heng-Tang, Schumaker V. N. Antigen valence and Fc-localized secondary forces in antibody precipitation. Mol Immunol. 1980 Dec;17(12):1591–1597. doi: 10.1016/0161-5890(80)90185-6. [DOI] [PubMed] [Google Scholar]
- Steensgaard J., Johansen A. S., Jacobsen C. On the composition of IgG anti-IgG immune complexes. Immunology. 1979 Dec;38(4):697–704. [PMC free article] [PubMed] [Google Scholar]
- Steensgaard J., Moller N. P., Funding L. The effects of overloading in density-gradient centrifugation. Eur J Biochem. 1975 Feb 21;51(2):483–493. doi: 10.1111/j.1432-1033.1975.tb03948.x. [DOI] [PubMed] [Google Scholar]
- Steward M. W., Petty R. E. The use of ammonium sulphate globulin precipitation for determination of affinity of anti-protein antibodies in mouse serum. Immunology. 1972 May;22(5):747–756. [PMC free article] [PubMed] [Google Scholar]
- Stewart G. A., Johns P. Empirical and theoretical relationships between the sedimentation coefficient and molecular weight of various proteins, with particular reference to the immunoglobulins. J Immunol Methods. 1976 Mar;10(2-3):219–229. doi: 10.1016/0022-1759(76)90173-3. [DOI] [PubMed] [Google Scholar]
