Antigenicity of modified .BETA.-lactoglobulin examined by three different assays
| Autor: | Shuichi Kaminogawa, Makoto Hattori, Jun-ichi Kurisaki, Shuji Nakamura, Kunio Yamauchi, Keiko Hotta, Soichiro Watanabe |
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| Rok vydání: | 1985 |
| Předmět: |
Antigenicity
Chromatography biology Chemistry food and beverages Chemical modification Radioimmunoassay General Biochemistry Genetics and Molecular Biology Immunodiffusion Succinylation Biochemistry Antigen biology.protein Antibody General Agricultural and Biological Sciences Quantitative analysis (chemistry) |
| Zdroj: | Agricultural and Biological Chemistry. 49:1733-1737 |
| ISSN: | 1881-1280 0002-1369 |
| DOI: | 10.1271/bbb1961.49.1733 |
| Popis: | The effects of chemical modifications on the antigenic properties of bovine β-lactoglobulin was studied by three different assay systems with IgG antibodies; immuno-double diffusion, quantitative immunoprecipitin assay, and radioimmunoassay. Carboxymethylation, succinylation, and guanidination seemed not to disturb the antigenicity of β-lactoglobulin in immuno-double diffusion, but the decrease in the affinity of these derivatives for anti-β-lactoglobulin antibody was observed in the quantitative immunoprecipitin assay and radioimmunoassay. Nitrophenylsulfenylation or reduction and Carboxymethylation seemed to delete one of the antigenic sites of β-lactoglobulin judging from the data of immuno-double diffusion, but the results from the quantitative immunoprecipitin assay and radioimmunoassay showed that reduction and Carboxymethylation affected the antigenicity of β-lactoglobulin more strongly than nitrophenylsulfenylation did. |
| Databáze: | OpenAIRE |
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