Interactions of the cytoprotective agent nocloprost (9 beta-chloro-16,16-dimethyl-prostaglandin E2, CAS 79360-43-3) with the microsomal monooxygenase system were studied in rat and human liver. Nocloprost did neither bind to human and rat liver cytochrome P-450 nor changed the activities of aniline hydroxylase, aminopyrine demethylase, ethylmorphine N-demethylase, 7-ethoxycoumarin and 7-ethoxyresorufin O-deethylase as well as 7-pentylresorufin O-depentylase after in vitro incubation with 1 ng/ml. Premedication of rats with 0.1 and 1.0 mg/kg lacked significant interferences with the monooxygenases studied.
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