It has been reported by several persons, including one of the authors, that DPNH obtained by the electrolytic reduction at controlled potentials is not fully active in respect to the reaction with alcohol dehydrogenase system. But statements concening the percentage of activity and the conditions which affect the activity were not identical. This article deals with these problems by reducing DPN electrolytically under different conditions followed by enzymatic examinations. The electrolytic reductions Of TPN and cytochrome c were also performed. Though the data presented are rather complicated, the most active DPNH was prepared in tripolyphosphate buffer with platinum electrode at −2.0 volt vs. S.C.E., under ice-cooling. The effects of phosphates and electrolytic potential are discussed.
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Kôno et al. (1958) studied this question.