The site of inhibition of porphyrin biosynthesis by an isomer of diazinon in rats.
2-Isopropyl-6-methyl-4-S-pyrimidinyl diethyl thiophosphate (isodiazinon) has been synthesized by an unambiguous route. Rats treated with isodiazinon over a 100-day period show decreased levels of liver ferrochelatase. Rats treated with diazinon and isodiazinon in combination over the same period show a more marked decrease in liver ferrochelatase activity as well as a decrease in the activity of coproporphyrinogen oxidase. Treatment of rats with stabilised diazinon over the same period is not associated with a decrease in the activity of either enzyme. Neither diazinon nor isodiazinon causes a decrease in the activity of glutamate dehydrogenase, succinate dehydrogenase or kynurenine hydroxylase, suggesting that the effect is specific to the porphyrin biosynthesis pathway and not due to mitochondrial damage.[1]References
- The site of inhibition of porphyrin biosynthesis by an isomer of diazinon in rats. Nichol, A.W., Elsbury, S., Angel, L.A., Elder, G.H. Biochem. Pharmacol. (1983) [Pubmed]
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