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By Gerald Litwack

Biochemical activities of Hormones V4

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This appears to result from an inhibition of androgen biosynthesis, rather than from an effect on the prostate itself. 2. 62). , 1973a). At higher pH, however, the iodoestrone rapidly inactivates the dehydrogenase. Both estradiol and NADP act as protectors against inactivation, and the alkylation process exhibits a rate saturation effect consistent with 16 John A. Katzenellenbogen 8 9α R=R' = 0 9b R = OH,R'=H an affinity labeling mechanism. Fluorescence and gel filtration studies indicate that the modified enzyme binds neither coenzyme nor substrate.

Two acetylenic 5,10-secosteroids (3a,b), which are unusual irreversible inhibitors of the isomerase of the "suicide" or fccat type (Rando, 1974a,b), have recendy been studied by Batzold and Robinson (1975) (Fig. 2). The structure of these agents was patterned after the ßyyacetylenic thiol esters used by Bloch (1969) in inhibitor studies of bacterial enzymes involved in the biosynthesis of unsaturated fatty acids. John A. 12 Katzenellenbogen 6/3-Bromo(la) 6a-Bromo(lb) FIG. 1. Representation of the active site of the A5-3-ketosteroid isomerase enzyme (B = basic residue, AH = acidic residue).

The obvious flexibility inherent in the external control of reactivity with the photoaffinity labeling 6 John A. Katzenellenbogen reagents (dark versus irradiation) allows one to arrange for conditions that should be optimal for labeling selectivity. But of greater importance is the fact that the covalent bond formation with conventional affinity labeling reagents (alkylation and acylation) involves reactions with sufficiently high activation energies to make them slow relative to the rates of complex formation and dissociation.

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