Heterologous expression and functional characterization of thioredoxin from Fasciola hepatica
| Autor: | José M. Martín-Alonso, Mara Salazar-Calderón, Arantxa D. Ruiz de Eguino, Francisco Parra |
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| Rok vydání: | 2001 |
| Předmět: |
Recombinant Fusion Proteins
Genetic Vectors Immunoblotting Molecular Sequence Data Heterologous Molecular cloning medicine.disease_cause Antioxidants Thioredoxins Glutamate-Ammonia Ligase Hepatica parasitic diseases Escherichia coli medicine Animals Insulin Amino Acid Sequence Genetics Expression vector General Veterinary biology Gene Transfer Techniques Peroxiredoxins General Medicine DNA Helminth Fasciola hepatica Blotting Northern biology.organism_classification Fusion protein Neoplasm Proteins Infectious Diseases Peroxidases Biochemistry Insect Science Electrophoresis Polyacrylamide Gel Parasitology Rabbits Heterologous expression Thioredoxin Oxidation-Reduction Sequence Alignment |
| Zdroj: | Parasitology Research. 87:390-395 |
| ISSN: | 1432-1955 0932-0113 |
| DOI: | 10.1007/s004360000353 |
| Popis: | The full thioredoxin coding sequence from Fasciola hepatica has been cloned into the pGEX-2T expression vector and produced in Escherichia coli as a fusion protein. The recombinant protein proved to be biologically active, using an insulin reduction assay, and was also able to activate thioredoxin peroxidase from F. hepatica. These observations suggest that this protein could participate in a redox cascade involved in the maintenance of cell homeostasis as well as in parasite protection against reactive oxygen species produced by the host. |
| Databáze: | OpenAIRE |
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