Purification and properties of the 3α-hydroxy steroid-dependent nicotinamide-adenine dinucleotide transhydrogenase of rat liver

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Abstract
3[alpha]-Hydroxy steroid-dependent nicotin-amide-adenine dinucleotide transhydrogenase from rat liver, partially purified by ammonium sulphate fractionation and column chromatography on diethylaminoethylcellulose, is activated by some bivalent anions. The effect of SO42- ions on the optimum H+ ion, steroid and NADP concentrations of the system, and on the reversibility of the reaction, have been examined. Some effects of the SO42- ions on NAD- and NADP-linked androsterone-dehydrogenase activity have also been studied.