Surface physicochemical properties of globulin-P amaranth protein
| Autor: | M. Cristina Añón, O. F. Castellani, Paula Aphalo, E. Nora Martínez |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Globulin
Chemical Phenomena Amaranth Enzyme-Linked Immunosorbent Assay Biology medicine.disease_cause Cross-reactivity Binding Competitive chemistry.chemical_compound Antibody Specificity Immunochemistry medicine Storage protein Plant Proteins chemistry.chemical_classification Chromatography Amaranthus Chemistry Physical Immune Sera Globulins General Chemistry Amaranthaceae biology.organism_classification Polymerization chemistry Biochemistry Seeds biology.protein Electrophoresis Polyacrylamide Gel Antibody General Agricultural and Biological Sciences |
| Zdroj: | Journal of agricultural and food chemistry. 52(3) |
| ISSN: | 0021-8561 |
| Popis: | Globulin-P, the polymerized 11S amaranth globulin, is composed of 280 kDa unitary molecules (UM, 23%) and aggregates larger than 500 kDa (A, 70%). Antibodies against these proteins were prepared to study their surface characteristics and to assess their homology with other storage proteins. Results showed that globulin-P unitary molecules and aggregates had similar reactive surfaces. A polypeptide of 56 kDa was found to be the most reactive to the antibodies assayed, followed by the acidic polypeptides. Such results support previous information, according to which these polypeptides appeared to be the most exposed on the molecule surface. Globulin-P fraction presented cross-reactivity with the remaining amaranth protein fractions: 11S-globulin, glutelins, and albumins. Globulin-P and 11S-globulin showed similar reactive surfaces whereas glutelin and albumins presented a lower cross-reactivity. The reactivity of the glutelin fraction depended on its sequence. Globulin-P fraction presented cross-reactivity with quinoa globulins, and to a lesser extent with globulins of sunflower and rice. Moreover, the anti-Gp serum was unable to detect either conformational or sequence epitopes in globulins of soybean, wheat, buckwheat, rice, and rye. |
| Databáze: | OpenAIRE |
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