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- W1567268979 abstract "Abstract 16α-Hydroxysteroid dehydrogenase, an estrogen-induced, soluble enzyme from rat kidneys, has been concentrated, partially purified, and separated from 16β- and 17β-hydroxysteroid dehydrogenase activities by a carboxymethyl cellulose column fractionation procedure. Spectrophotometric measurement of the reduction of 3,17β-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 16α-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." @default.
- W1567268979 created "2016-06-24" @default.
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- W1567268979 date "1966-09-01" @default.
- W1567268979 modified "2023-09-28" @default.
- W1567268979 title "16α-Hydroxysteroid Dehydrogenase of Rat Kidney" @default.
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- W1567268979 doi "https://doi.org/10.1016/s0021-9258(18)99804-2" @default.
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