4-hydroxy-5-nitrophenyl-acetic-acid has been researched along with Hemolysis* in 2 studies
2 other study(ies) available for 4-hydroxy-5-nitrophenyl-acetic-acid and Hemolysis
| Article | Year |
|---|---|
Comparison of the effector functions of human immunoglobulins using a matched set of chimeric antibodies.
Cell lines have been established that secrete a matched set of human chimeric IgM, IgG1, IgG2, IgG3, IgG4, IgE, and IgA2 antibodies that are directed against the hapten 4-hydroxy-3-nitrophenacetyl. These chimeric antibodies secreted from mouse plasmacytoma cells behave exactly like their authentic human counterparts in SDS-PAGE analysis, binding to protein A and in a wide range of serological assays. The antibodies have been compared in their ability to bind human C1q as well as in their efficacy in mediating lysis of human erythrocytes in the presence of human complement. A major conclusion to emerge is that whereas IgG3 bound C1q better than did IgG1, the chimeric IgG1 was much more effective than all the other IgG subclasses in complement-dependent hemolysis. The IgG1 antibody was also the most effective in mediating antibody-dependent cell-mediated cytotoxicity using both human effector and human target cells. These results suggest that IgG1 might be the favoured IgG subclass for therapeutic applications. Topics: Animals; Antibodies, Monoclonal; Antibody-Dependent Cell Cytotoxicity; Cell Line; Complement Activating Enzymes; Complement C1; Complement C1q; Complement System Proteins; DNA, Recombinant; Electrophoresis, Polyacrylamide Gel; Genes, Immunoglobulin; Glycosylation; Haptens; Hemolysis; Humans; Immunoglobulins; Mice; Nitrophenols; Phenylacetates; Plasmacytoma; Plasmids; Transfection; Tumor Cells, Cultured | 1987 |
Low affinity of kappa chain bearing (4-hydroxy-3-nitrophenyl)acetyl (NP)-specific antibodies in the primary antibody repertoire of C57BL/6 mice may explain lambda chain dominance in primary anti-NP responses.
The primary anti-(4-hydroxy-3-nitrophenyl)acetyl (anti-NP) antibody response of C57BL/6 mice was analyzed by several methods. Serum analyses by solid-phase radioimmunoassay (RIA) showed that stimulation with the thymus-independent (TI) type 1 antigen NP-LPS results in an anti-NP antibody response dominated by kappa (kappa) light chain bearing antibodies, whilst responses to NP-Ficoll (a TI-2 antigen) and NP-KLH (a thymus dependent antigen) are dominated by lambda (lambda) 1 light chain bearing antibodies. However, in all these responses NP-specific plaque-forming cells (PFCs) were predominantly heteroclitic, and inhibitable by anti-lambda antiserum. In addition, kappa-bearing IgM-producing hybridomas obtained by fusion of spleen cells from NP-LPS-immunized mice, although producing NP-specific antibodies detectable by RIA, were unable to produce NP-specific plaques. Direct determination of the affinity of 5 of those hybridomas by fluorometric titrations showed that their affinity is indeed lower than 10(-5) M. These results suggest that most NP-specific antibodies stimulated by NP-LPS are of too low affinity to be detected in a direct PFC assay, with the exception of a population of lambda-bearing antibodies. Therefore, the differential expression of kappa- or lambda-bearing antibodies in primary responses to the hapten NP presented on different carriers may be due to different affinity requirements for B-cell triggering via different activation pathways. Topics: Animals; Antibody Affinity; Haptens; Hemolysis; Hemolytic Plaque Technique; Immunoglobulin kappa-Chains; Immunoglobulin lambda-Chains; Immunoglobulin Light Chains; Mice; Mice, Inbred C57BL; Nitrophenols; Phenylacetates; Radioimmunoassay | 1985 |