Abstract
Salazar-Calderón, M., Martín-Alonso, J. M., Ruiz de Eguino, A. D., Casais, R., Marín, M. S., and Parra, F. 2000. Fasciola hepatica: Heterologous expression and functional characterization of a thioredoxin peroxidase. Experimental Parasitology95, 63–70. A Fasciola hepatica cDNA clone of 779 bp was isolated from an adult worm cDNA expression library by immunological screening using a rabbit serum against the excretory–secretory antigens. The nucleotide sequence of the cDNA revealed the presence of an open reading frame of 582 bp which encoded a 194-amino-acid-residue polypeptide (Mr 21,723 Da) showing a high degree of homology to thioredoxin peroxidases. This putative antioxidant protein gene was expressed in Escherichia coli as a GST fusion protein. The recombinant fusion protein showed in vitro antioxidant properties and protected rabbit muscle enolase and E. coli glutamine synthetase from inactivation by nonenzymatic Fe3+/O2/DTT or Fe3+/O2/ascorbate metal-catalyzed oxidation systems.
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