Abstract
It has become clear that the reduced coenzyme I (NADH) produced by malic dehydrogenase is oxidized by Diaphorase I but the route by which NADH is oxidized in the murine leprosy bacillus is not know. Since there is no cytochrome system in the murine leprosy bacillus, catalyzation by oxygen in air will not take place. In cultivating the organism in vitro, a pathway for the hydrogen of NADH must be made inorder that energy may be produced, else cultivation is not possible. Elucidation of the conditions which will adequately fulfil the flow of electrons will become an important starting point for the in vitro cultivation of the murine leprosy bacillus.
As the initial step, it has been found that NADH is converted to NAD and water by NADH peroxydase in the presence of H2O2. This NADH peroxydase is present not only in murine leprosy bacillus but is also present in vitro cultivated M. Jucho and BCG. The enzyme is easily inactivated by heat but is stable to dialysis.
When the murine leprosy bacillus is present in the host cell, H2O2 is produced by the cell so the flow of electrons may proceed smoothly and energy produced through the action of NADH peroxydase but utilization of this pathway is difficult in vitro.
