
doi: 10.1159/000302030
The effects of two organic mercurials (4-acetatomercuri-17Β-estradiol and <i>p</i>-chloromercuribenzoate) on human placental estradiol dehydrogenase were evaluated by equilibrium rate exchange and initial velocity measurements. The steroid mercurial was more effective in reducing isotopic exchange between steroid pairs than between cosubstrate pairs. An opposite result was obtained using <i>p</i>-chloromercuribenzoate. The results suggest that the mercury estradiol is useful as an affinity label for the steroid binding site of this class of enzymes.
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