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Patrick B. Kyle, Stanley V. Smith, Rodney C. Baker and Robert E. Kramer Mass spectrometric detection of CYP450 adducts following oxidative desulfuration of methyl parathion Journal of Applied Toxicology 33

Version of Record online: 23 JAN 2012 | DOI: 10.1002/jat.1792

Cytochrome P450-mediated desulfuration of organophosphorus compounds results in mechanism-based enzyme inhibition. Data suggest that reactive sulfur is released and binds to the apoprotein, although the identities of neither the adduct(s) nor the affected amino acid(s) have been clearly determined. In this work, 96 amu adducts to two cysteines of rat CYP3A1 were determined after incubation with methyl parathion. These adducts correspond to the mass of three sulfur atoms, as well as combinations of sulfur and oxygen.

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