Specificity of IgM Antibodies to Pooled Human F(ab')2Fragments
| Autor: | John L. Abruzzo, Lawrence D. Wolfe, Ralph Heimer |
|---|---|
| Rok vydání: | 1984 |
| Předmět: |
Igm antibody
Immunology Radioimmunoassay Enzyme-Linked Immunosorbent Assay Endogeny Cross Reactions Immunoglobulin light chain Arthritis Rheumatoid Epitopes Immunoglobulin Fab Fragments Antigen Antibody Specificity Rheumatoid Factor medicine Humans Genetics medicine.diagnostic_test biology Chemistry medicine.disease Molecular biology Primary and secondary antibodies Immunoglobulin M Immunoglobulin G Immunoassay Rheumatoid arthritis biology.protein Antibody |
| Zdroj: | Immunological Communications. 13:15-27 |
| ISSN: | 0090-0877 |
| DOI: | 10.3109/08820138409025446 |
| Popis: | An isotope specific immunoassay which minimizes interference by endogenous rheumatoid factors was used to determine the specificity of IgM anti-F(ab')2 antibodies in human serum. We underscore the heterogeneity of these antibodies. While one subset of IgM anti-F(ab')2 antibodies reacts only with intact F(ab')2, another recognizes determinants present following reduction and alkylation of F(ab')2 and separation of Fd' fragments from light chains. IgM anti-F(ab')2 antibodies in sera from rheumatoid arthritis patients do not react significantly with intact pooled IgG and, therefore, probably are not anti-idiotypic antibodies. Some sera, but not all, contain elevated levels of antibodies that are crossreactive with rabbit F(ab')2. Such crossreactive antibodies may interfere with assays which utilize F(ab')2 fragments of rabbit antibodies specific for antigens of clinical relevance. |
| Databáze: | OpenAIRE |
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