Human IgG3 can adopt the disulfide bond pattern characteristic for IgG1 without resembling it in complement mediated cell lysis
- 30 November 1993
- journal article
- Published by Elsevier BV in Molecular Immunology
- Vol. 30 (16), 1419-1425
- https://doi.org/10.1016/0161-5890(93)90103-i
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- The extended hinge region of IgG3 is not required for high phagocytic capacity mediated by Fcγ receptors, but the heavy chains must be disulfide bondedEuropean Journal of Immunology, 1993
- Role of inter-heavy and light chain disulfide bonds in the effector functions of human immunoglobulin IgG1Molecular Immunology, 1992
- Chimeric mouse human IgG3 antibodies with an IgG4-like hinge region induce complement-mediated lysis more efficiently than IgG3 with normal hingEuropean Journal of Immunology, 1991
- Human IgG subclass pattern of inducing complement‐mediated cytolysis depends on antigen concentration and to a lesser extent on epitope patchiness, antibody affinity and complement concentrationEuropean Journal of Immunology, 1991
- Enhancement of Complement Activation and Cytolysis of Human IgG3 by Deletion of Hinge ExonsScandinavian Journal of Immunology, 1990
- C1q binding to chimeric monoclonal IgG3 antibodies consisting of mouse variable regions and human constant regions with shortened hinge containing 15 to 47 amino acidsEuropean Journal of Immunology, 1989
- Cytotoxicity mediated by human Fc receptors for IgGImmunology Today, 1989
- Comparison of the effector functions of human immunoglobulins using a matched set of chimeric antibodies.The Journal of Experimental Medicine, 1987
- The Binding of Human Immunoglobulin G1 Monomer and Small, Covalently Cross-Linked Polymers of Immunoglobulin G1 to Human Peripheral Blood Monocytes and Polymorphonuclear LeukocytesJCI Insight, 1982
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970