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glutathione peroxidase chemical structure Unglycosylated recombinant human 3 mutant from Escherichia coli is active as a monomer General reaction mechanisms for antioxidant
glutathione peroxidase chemical structure Unglycosylated recombinant human 3 mutant from Escherichia coli is active as a monomer General reaction mechanisms for antioxidant
glutathione peroxidase chemical structure Unglycosylated recombinant human 3 mutant from Escherichia coli is active as a monomer General reaction mechanisms for antioxidant
glutathione peroxidase chemical structure Unglycosylated recombinant human 3 mutant from Escherichia coli is active as a monomer General reaction mechanisms for antioxidant
glutathione peroxidase chemical structure

glutathione peroxidase chemical structure Unglycosylated recombinant human 3 mutant from Escherichia coli is active as a monomer General reaction mechanisms for antioxidant

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Activities of GST and some antioxidative enzymes were markedly induced 57 days after inoculation in susceptible barley leaves

glutathione peroxidase chemical structure Unglycosylated recombinant human 3 mutant from Escherichia coli is active as a monomer General reaction mechanisms for antioxidant

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glutathione peroxidase chemical structure Unglycosylated recombinant human 3 mutant from Escherichia coli is active as a monomer General reaction mechanisms for antioxidant

For number and definition of replicates for experimental approaches, please see the corresponding Methods sections

glutathione peroxidase chemical structure Unglycosylated recombinant human 3 mutant from Escherichia coli is active as a monomer General reaction mechanisms for antioxidant

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glutathione peroxidase chemical structure Unglycosylated recombinant human 3 mutant from Escherichia coli is active as a monomer General reaction mechanisms for antioxidant

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glutathione peroxidase chemical structure Unglycosylated recombinant human 3 mutant from Escherichia coli is active as a monomer General reaction mechanisms for antioxidant
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