Heterologous expression and functional characterization of thioredoxin from Fasciola hepatica
2001
Salazar-Calderón, Mara | Martín-Alonso, José M. | Ruiz de Eguino, Arantxa D. | Parra, Francisco
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.
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