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16agr-Hydroxysteroid Dehydrogenase of Rat Kidney

PURIFICATION, ASSAY, AND PROPERTIES

Robert A. Meigs 1 and Kenneth J. Ryan 1

From the 1 From the Department of Obstetrics and Gynecology, Western Reserve University School of Medicine, Cleveland, Ohio 44106

16agr-Hydroxysteroid dehydrogenase, an estrogen-induced, soluble enzyme from rat kidneys, has been concentrated, partially purified, and separated from 16ß- and 17ß-hydroxysteroid dehydrogenase activities by a carboxymethyl cellulose column fractionation procedure. Spectrophotometric measurement of the reduction of 3,17ß-dihydroxyestra-1,3,5(10)-trien-16-one to estriol by reduced nicotinamide adenine dinucleotide has been employed to assay and characterize the purified enzyme. This preparation catalyzes the specific interconversion of 16agr-hydroxy- and 16-ketosteroids. Its pH optimum for steroid reduction is 6.1 to 6.2, and it is inhibited by low concentrations of heavy metal ions, reagents which modify sulfhydryl groups, and metal chelators. At the present state of enzyme purity, a number of phenolic C18 and neutral C19 steroids can serve as substrates, and nicotinamide adenine dinucleotide phosphate can replace nicotinamide adenine dinucleotide as cofactor. This enzyme is distinguished by its specificity from similar hydroxysteroid dehydrogenases previously characterized and has been utilized as a stereospecific reagent for substrate synthesis.

Submitted on March 28, 1966


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Copyright © 1966 by the American Society for Biochemistry and Molecular Biology.
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