Abstract
Inhibition of aromatase activity in human placental microsomes with 3-deoxy-(1, 2, 4, 6 and 8), 6-oxo-(3, 5 and 9), and 16α-bromo- (7) steroids was studied using [1β- 3H]16α- hydroxyandrostenedione (16α-OHAD) as a substrate and compared to that with the conventional substrate, [1β- 3H]androstenedione. All the steroids inhibited both 16α-OHAD and [1β- 3H]androstenedione aromatization in a competitive manner. Based on K i / K m ratios obtained in both series of experiments, their relative inhibitory activities in the series with 16α-OHAD were not necessarily identical with those in the other series. The results would be important to understand the relationship of structure to function of aromatase in human placental microsomes.
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More From: Journal of Steroid Biochemistry and Molecular Biology
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