Chromatographic purification and characterization of elicitors of necrosis on tabacco produced by incompatible Phytophthora species
| Autor: | G. Michel, Jean-Claude Huet, Jean-Claude Pernollet, M. Bruneteau, G. Richard, A. Vergne, Pierre Ricci, V. Billard, Ph. Bonnet |
|---|---|
| Přispěvatelé: | Station de botanique et de pathologie végétale, Institut National de la Recherche Agronomique (INRA), Unité de recherche Nutrition Azotée des Plantes (URNAP), ProdInra, Migration |
| Jazyk: | angličtina |
| Rok vydání: | 1988 |
| Předmět: |
0106 biological sciences
0303 health sciences Chromatography [CHIM.ANAL] Chemical Sciences/Analytical chemistry biology Chemistry Phytophthora cryptogea Organic Chemistry Size-exclusion chromatography General Medicine Phytophthora cinnamomi biology.organism_classification 01 natural sciences Biochemistry Analytical Chemistry Elicitor 03 medical and health sciences Phytophthora capsici Sephadex [CHIM.ANAL]Chemical Sciences/Analytical chemistry Phytophthora Polyacrylamide gel electrophoresis ComputingMilieux_MISCELLANEOUS 030304 developmental biology 010606 plant biology & botany |
| Zdroj: | Journal of Chromatography A Journal of Chromatography A, Elsevier, 1988, 44, pp.87-94 |
| ISSN: | 0021-9673 1873-3778 |
| Popis: | A chromatographic procedure was developed to purify the proteins eliciting necrosis in tobacco and produced in culture by three species of Phytophthora: cryptogein from P. cryptogea, cinnamomin from P. cinnamomi and capsicin from P. capsici. The procedure included ion-exchange chromatography and gel filtration on Sephadex G-25. Polyacrylamide gel electrophoresis data and the amino acid composition are in agreement with a molecular mass near 10 000 for these proteins. Their behaviour on ion-exchange columns indicates that cryptogein and cinnamomin are basic proteins and capsicin an acidic one. In biological tests on excised tobacco leaf, cryptogein and cinnamomin exhibited an activity 50–100-fold that of capsicin. |
| Databáze: | OpenAIRE |
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