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Antioxidative catalytic activities of trans-3,4-dihydroxyselenolane (DHS red ), a water-soluble cyclic selenide, were investigated in the reaction of hydrogen peroxide with three different thiol substrates, monothiol glutathione (GSH), dithiol dithiothreitol (DTT red ), and polythiol reduced ribonuclease A (RNase A) having eight thiol groups along the polypeptide chain. For all the thiol substrates, DHS red exhibited higher glutathione peroxidase (GPx)-like antioxidative catalytic ac-

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