Abstract
In vitro experiments have indicated the presence of a microsomal enzyme system in rat liver which is capable of converting various simple monoalkylhydrazines to their parent hydrocarbons, as determined by gas chromatography. These reactions were found to require oxygen and a NADPH-regenerating system for maximum activity. In the absence of a NADPH-regenerating system, the oxidized forms of FAD, FMN, and NADP enhanced the rate of the reaction. Methylhydrazine was converted to methane at a rate of ~1.0 mμmole/120 min/mg microsomal protein. Reactivity appeared to be nearly the same for the following hydrazines: Methyl-, ethyl-, n-propyl-, isopropyl-, and n-butylhydrazine. The requirement for NADPH and oxygen suggests that the enzyme may be related to other NADPH-dependent oxidases in the microsomes.
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