Abstract
Cellular localization of two cytochrome P-450-dependent monooxygenase activities (7-ethoxycoumarin deethylase and coumarin hydroxylase) in the mouse lung was examined with the dispersed cells, which were fractionated on a Percoll isopycnic gradient and identified by electron microscopy. The 7-ethoxycoumarin deethylase activity was widely distributed in various types of lung cells. The coumarin hydroxylase activity, on the other hand, was almost exclusively localized in Clara cell-rich fractions (80% purity) in terms of both total and specific activities. Because coumarin hydroxylase is associated with cytochrome P-450, reportedly involved in the activation of various procarcinogens and necrotoxic substances, a high frequency of chemically induced cancer and necrosis in Clara cells may, at least in part, be explained by the exclusive localization of this enzyme activity in this type of cells.
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