Purification and Characterisation of Two GST'S Forms from Rhizobium Leguminosarum with a High Affinity to Herbicides
| Autor: | Domenico Paludi, B. Dainelli, Antonio Aceto, A. Faraone, M. Petrucci |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Functional role
Immunology Cell Endogeny medicine.disease_cause Rhizobium leguminosarum Glutathione transferase 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Bacterial Proteins medicine Immunology and Allergy Glutathione Transferase Pharmacology chemistry.chemical_classification Herbicides food and beverages Glutathione Isoenzymes Kinetics Cytosol Enzyme medicine.anatomical_structure chemistry Biochemistry 030220 oncology & carcinogenesis Protein Binding 030215 immunology |
| Zdroj: | International Journal of Immunopathology and Pharmacology. 16:55-60 |
| ISSN: | 2058-7384 |
| DOI: | 10.1177/039463200301600108 |
| Popis: | Cytosolic glutathione transferase are a family of multifunctional proteins that catalyse the conjugation of GSH to a large variety of endogenous and exogenous compounds. These enzymes have been widely studied in mammals and, to a lesser extent, in plants. In plants, GSTs can detoxify herbicides; they are also induced by pathogenic infection and are likely to be involved in defence responses. GSTs are found in pathogenic and not pathogenic prokaryotes but the functional role played by these enzymes in the cell still remains to be clarified. Here, we report the purification and characterisation of two GST's forms from Rhizobium leguminosarum that play a very important role in agriculture by inducing nitrogen-fixing nodules on the roots of legumes. These bacterial GSTs from R. leguminosarum have immunological characteristics that are different among them and they are characterised both by a high affinity to herbicides. |
| Databáze: | OpenAIRE |
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