Highly purified preparations of the 4‐en‐3‐oxosteroid: (acceptor)‐1‐en‐oxidoreductase from Nocardia opaca have been investigated in both types of reactions: 1.2‐dehydrogenation of the 4‐en‐3‐oxo‐derivative and 1.2‐hydrogenation of the 1.4‐dien‐3‐oxo‐derivative. It was not possible to separate the hydrogenating activity from the dehydrogenating activity by affinity chromatography, disc electrophoresis, SDS‐electrophoresis, and isoelectric focusing techniques. The pure enzyme preparation is discussed as only one FAD depending protein acting in response to the system as a dehydrogenase as well as a reductase.
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