Non-immune VH-binding Specificity of Human Protein Fv
| Autor: | S. Iscaki, Jean-Pierre Bouvet, Canh P. Quan, Jacques Pillot, René Pires |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Sialoglycoproteins
Dimer Immunology Immunoglobulins Enzyme-Linked Immunosorbent Assay Immunoglobulin light chain Guanidines Epitope Epitopes chemistry.chemical_compound Humans Guanidine Chromatography High Pressure Liquid Binding selectivity chemistry.chemical_classification Lymphokines biology Binding protein General Medicine Hepatitis C Molecular biology Dithiothreitol Enzyme chemistry biology.protein Immunoglobulin Light Chains Antibody Immunoglobulin Heavy Chains |
| Zdroj: | Scandinavian Journal of Immunology. 33:381-386 |
| ISSN: | 1365-3083 0300-9475 |
| DOI: | 10.1111/j.1365-3083.1991.tb01785.x |
| Popis: | The specificity of human F(ab)-binding Protein Fv (previously called Protein F), a sialoprotein released into the digestive tract mainly during hepatitis, was investigated with fragments or chains of monoclonal immunoglobulins. Protein Fv bound an unreduced H-chain dimer of a monoclonal human IgA2m(1) molecule but neither the corresponding L-chain dimer, nor several Bence-Jones molecules. Using enzymatic subfragments of F(ab)mu, or F(ab')2 gamma, a significant binding was observed with Fv fragments (VH + VL), while Fb fragments (CH1 + CL) were inactive. Taken altogether, these results prove that the structure recognized by Protein Fv is located in the VH domain. This structure probably involves discontinuous epitopes linked by a disulphide bond, which are destroyed by combined reduction and dissociation. Protein Fv does not interfere with the antigen-binding site, since there was no reciprocal inhibition with the antigen-antibody reaction. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text