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- W1993583532 abstract "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 (M(r) 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 Fe(3+)/O(2)/DTT or Fe(3+)/O(2)/ascorbate metal-catalyzed oxidation systems." @default.
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- W1993583532 date "2000-05-01" @default.
- W1993583532 modified "2023-09-25" @default.
- W1993583532 title "Fasciola hepatica: Heterologous Expression and Functional Characterization of a Thioredoxin Peroxidase" @default.
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- W1993583532 doi "https://doi.org/10.1006/expr.2000.4495" @default.
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