Abstract
E. coli thioredoxin plus thioredoxin reductase have previously been shown to replace dithiothreitol as the electron donor for mammalian liver microsomal vitamin K epoxide reduction in vitro. Such activity is dependent on detergent disruption of the microsomal membrane integrity. A previously characterized salicylate-inhibitable pathway for electron transfer from endogenous cylosolic reducing agents to the microsomal epoxide reducing warfarin-inhibitable enzyme is not inhibited by known alternate substrates and inhibitors of the thioredoxin system nor by antibodies against thioredoxin.
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