The effect of RMI 12,936, a synthetic antiprogestational steroid, on ovarian steroidogenesis in the rat

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Abstract
A series of physiochemical investigations confirmed that the product of chemical and enzymatic isomerization of RMI 12,936 [17.beta.-hydroxy-7.alpha.-methylandrost-5-en-3-one] was 7.alpha.-methyltestosterone. The total activity per pair of ovaries of .DELTA.5 3-ketosteroid isomermase in vitro was unchanged by RMI 12,936 pretreatment or by advancing pregnancy, significant changes in ovarian weight being accompanied by reciprocal changes in enzyme activity/mg tissue. The initial linear rate of isomerization of RMI 12,936 was approximately 5 times greater than the corresponding rate of .DELTA.5-progesterone isomerization at equal substrate concentrations. RMI 12,936 probably does not inhibit progesterone biosynthesis by alteration of .DELTA.5 3-ketosteroid isomerase activity, but it may do so by acting as an alternative substrate for this enzyme.

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