IT HAS been reported (Samuels et al., 1951) that corpora lutea, placentae, interstitial cells of the testis, and the adrenal cortex contain an enzyme which would oxidize a 3β-hydroxy group in a steroid to a 3-ketone if the compound had an oxygen on C-17 or C-20. A wide range of other tissues, including the ovarian follicle, did not show this activity under the conditions studied. There did not seem to be any difference in specificity among the active tissues, since Δ5-pregnen-3β-ol-20-one was converted to progesterone and dehydroepiandrosterone was converted to Δ4-androstene-3,4-dione by homogenates of either the testis, placenta or adrenal. It appeared, therefore, that this enzyme played a basic role in the formation of the nonbenzenoid steroid hormones and that the distinction in the final product from each gland depended on other enzymic reactions.
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Samuels et al. (1956) studied this question.