Framework peptides fromxIIIb rheumatoid factor light chains with binding activity for aggregated IgG
| Autor: | Geysen Hm, Tribbick G, Soltys Aj, Frank C. Hay |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
chemistry.chemical_classification
Subfamily biology Molecular Sequence Data Immunology Peptide Immunoglobulin light chain Peptide Fragments Amino acid Immunoglobulin kappa-Chains Antigen Biochemistry chemistry Rheumatoid Factor Immunoglobulin G Monoclonal biology.protein Humans Immunology and Allergy Rheumatoid factor Immunoglobulin Light Chains Amino Acid Sequence Antibody |
| Zdroj: | European Journal of Immunology. 21:1837-1841 |
| ISSN: | 1521-4141 0014-2980 |
| DOI: | 10.1002/eji.1830210809 |
| Popis: | Most monoclonal human rheumatoid factors (RF) and some RF from rheumatoid patient's synovia are restricted in their light chains, using predominantly the kappa IIIb subfamily. Very few sequence differences are found between these light chains. Light chains with similar variable region framework sequences are also found in some mouse monoclonal RF derived from mice stimulated with lipopolysaccharide or secondarily immunized with protein antigens. There are two likely explanations for this restriction in framework sequences between the two species: (a) the sequences are important for the immunoregulation of RF production or (b) the sequences are concerned with the antibody binding specificity of the RF. We have examined overlapping octapeptides from the kappa IIIb light chain variable region and show that some framework peptides have the ability to bind aggregated IgG. Replacement of amino acids within the peak binding peptide have indicated the critical amino acids necessary for binding. |
| Databáze: | OpenAIRE |
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