Characterization of Deinococcus radiophilus thioredoxin reductase active with both NADH and NADPH

Abstract

Thioredoxin reductase (TrxR, EC 1.6.4.5) of Deinococcus radiophilus was purified by steps of sonication, ammonium sulfate fractionation, 2′5′ ADP Sepharose 4B affinity chromatography, and Sephadex G-100 gel filtration. The purified TrxR, which was active with both NADPH and NADH, gave a 368 U/mg protein of specific activity with 478-fold purification and 18… (More)
DOI: 10.1007/s12275-010-0283-7

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