Abstract
GLUTAMIC dehydrogenase (GDH) has been used as a model enzyme in the study of the interaction between steroid hormones and enzymes1. It was found that in experiments in vitro 17β-oestradiol, oestriol, oestrone and diethylstilboestrol (DES) inhibited the action of GDH, DES being the strongest inhibitor. During the past few years, clomiphene, that is, 1-[p-β-diethylaminoethoxy)-phenyl]-1,2-diphenyl-2-chloroethylene, 
has been applied to induce ovulation in anovulatory patients2, although the mechanism of its action is not yet fully understood. Comparison of the structures of DES (that is, α, α′-diethylenstilbestenediol) 
and clomiphene reveals some similarities: both compounds are derivatives of ethylene and both contain at least two phenyl groups.
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References
Yielding, K. L., and Tomkins, G. M., in Recent Progress in Hormone Research XVIII (edit. by Pincus, G.), 467 (Academic Press, New York, 1962).
Pildes, R. B., Amer. J. Obst. Gynec., 91, 466 (1965).
Schmidt, E., in Methoden der Enzymatischen Analysen (edit. by Bergmeyer, H-U.), 752 (Verlag Chemie, Weinheim, 1962).
Hofmann, K., in Recent Progress in Hormone Research XVIII (edit. by Pincus, G.), 488 (Academic Press, New York, 1962).
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PURANEN, J., ARSTILA, A. Inhibition of Glutamic Dehydrogenase by Clomiphene. Nature 213, 78–79 (1967). https://doi.org/10.1038/213078a0
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DOI: https://doi.org/10.1038/213078a0
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