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62821 
Journal Article 
The N-oxidation of alkylhydrazines catalyzed by the microsomal mixed-function amine oxidase 
Prough, RA 
1973 
Yes 
Archives of Biochemistry and Biophysics
ISSN: 0003-9861
EISSN: 1096-0384 
NIOSH/00129256 
158 
1 
442-444 
English 
4729304 
WOS:A1973Q577800052 
The catalytic effect of microsomal, mixed function amine-oxidase on reduced nicotinamide-adenine-dinucleotide-phosphate (NADPH) oxidation of the N-methylhydrazines was studied in-vitro. Substrates of dimethylaniline (121697), methylhydrazine (60344), 1,1-dimethylhydrazine (57147), 1,2-dimethylhydrazine (540738), and procarbazine (671169), were treated with mixed function amine-oxidase from pig liver and NADPH. Concentrations were 0.054 milligrams per milliliter for the mixed function amine-oxidase and 33 micromoles for NADPH. NADPH oxidation was monitored spectrophotometrically, and the evolution of methane was determined by gas chromatography. Reactions were studied at pH 7.7 and 25 degrees-C. Maximal oxidation rates were 154.0 nanomoles per minute per milligram protein for methylhydrazine, 107.1 for dimethylaniline, 86.9 for 1,1-dimethylhydrazine, and less than 36 for the other compounds. Michaelis constants ranged from 0.43 to 35.0 millimeters for the hydrazines, as compared to 0.014 for dimethylaniline. Methane production was observed when methylhydrazine was used as a substrate. The author concludes that mixed function amine-oxidase can oxidize alkylhydrazines in the presence of oxygen and NADPH. The formation of methane from methylhydrazine may be due to the decomposition of an N-oxidation intermediate. 
DCN-117911; Amines; Biochemical analysis; Biochemical tests; Enzymes; Enzyme activity; Enzyme complexes; Chromatographic analysis; Microsomal enzymes