Trypsin inhibitors fromPisum sativum L exhibit identical epitopes
| Autor: | J. Delort-Laval, Luu Phan Thanh, Alain Paraf, Thérèse Gaborit |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
Antiserum
Nutrition and Dietetics Chromatography biology medicine.diagnostic_test Trypsin inhibitor food and beverages Immunoelectrophoresis biology.organism_classification Trypsin Epitope Pisum Sativum Biochemistry Enzyme inhibitor biology.protein medicine Agronomy and Crop Science Food Science Biotechnology medicine.drug |
| Zdroj: | Journal of the Science of Food and Agriculture. 48:15-27 |
| ISSN: | 1097-0010 0022-5142 |
| DOI: | 10.1002/jsfa.2740480104 |
| Popis: | Pea (Pisum sativum L) trypsin inhibitor, known to be a mixture of at least eight different peptides exhibiting different charges as shown by electrophoresis, was subjected to an immunochemical analysis. By PAGE-SDS analysis, only one large diffuse band was detected showing that pea trypsin inhibitor peptides have a molecular weight between 12000 and 15000 amu. After preparative non-denaturing electrophoresis, four major bands, as judged by Coomassie blue staining, were purified and each of them was used to raise specific antibodies in rabbits. By ELISA test, immunoelectrophoresis and absorption on an immunoaffinity column, it was shown that each antiserum directed against any one of the four bands completely cross-reacted against each other. Thus, it can be concluded that each component of the pea trypsin inhibitor should exhibit a very strong sequence homology. |
| Databáze: | OpenAIRE |
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