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. 1983 Sep;18(3):500–504. doi: 10.1128/jcm.18.3.500-504.1983

Inactivation of contraceptive steroid hormones by human intestinal clostridia.

V D Bokkenheuser, J Winter, B I Cohen, S O'Rourke, E H Mosbach
PMCID: PMC270842  PMID: 6630441

Abstract

Steroid hormones reduced in ring-A are devoid of hormonal activity. In metabolic experiments we found that human fecal flora reduced the delta 4-3-keto structure of natural progestins to 3 alpha-hydroxy, 5 beta-steroid metabolites (3 alpha,5 beta) and of synthetic progestins to a mixture of 3 alpha,5 beta and 3 beta,5 beta compounds. 3 alpha,5 beta-Reductase was synthesized by Clostridium paraputrificum and had a strong affinity for natural progestins such as progesterone. 3 beta,5 beta-Reductase was synthesized by Clostridium innoculin and had a stronger affinity for synthetic progestins. A third enzyme, 3 beta,5 alpha-reductase, was synthesized by St. Luke's strain 209 (Clostridium species "J-1") but was only observed when pure cultures were used. Ring-A reduction of synthetic progestins was 3 to 10 times slower than that of natural progestins, thus explaining the pharmacological superiority of synthetic progestins over naturally occurring analogs.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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