Characterization of estrone hydroxylase activities in porcine endometrial cells
- 1 January 1994
- journal article
- research article
- Published by Georg Thieme Verlag KG in Experimental and Clinical Endocrinology & Diabetes
- Vol. 102 (05) , 388-393
- https://doi.org/10.1055/s-0029-1211309
Abstract
The oxidation of estradiol to estrone in porcine endometrial cells is succeeded by hydroxylation at either 6α- or 7α-. The products are devoid of receptor affinity. Their formation is inhibited by cytochrome P450 blockers like ketoconazol but not by chloroquine and analogues. The hydroxylation at 6α- proceeds with KM = 1.9 × 10−7 M, that at 7α- with KM = 3.6 × 10−7 M. The respective values for the cytochrome P450-reductase cosubstrate NADPH are 1.7 × 10−5 M and 1.9 × 10−5 M. The kinetic parameters of the enzymes are compatible with a metabolic sequence: estradiol → estrone → 6α-/7α-estrone.Keywords
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