Abstract
The effects of microsomal enzyme inhibitors (7, 8-BF and SKF 525-A) on the S-9-mediated mutagenicity of o-, m- and p-phenylenediamine were investigated using Salmonella typhimurium TA98. SKF 525-A did not affect the enzyme-mediated mutagenicity of m- and p-phenylenediamine, while 7, 8-BF reduced significantly the mutagenicity of all three isomers of phenylenediamine. When the enzyme reactions in the agar overlayer were stopped successively by adding 7, 8-BF directly onto the plate, the number of revertants increased linearly with time at least for 6 hours. These data suggest that cytochrome P-448 takes a main role in the activation of phenylenediamines and that in the agar layer this microsomal enzyme remain active for a period as long as 6 hours at 37 degrees C.
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