Purification and Properties of a Bovine Adrenal 21-Dehydrosteroid Reductase

An enzyme that catalyzes the reduction of 21-dehydrosteroids has been purified approximately 250-fold from acetone powder extracts of bovine adrenal glands. The reaction is specific for DPNH, but no structural requirements of substrate other than the steroid nucleus were evident. Steroids are compet...

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Veröffentlicht in:	The Journal of biological chemistry 1968-03, Vol.243 (6), p.1190-1197
Hauptverfasser:	Furfine, C S, White, A
Format:	Artikel
Sprache:	eng
Schlagworte:	17-Hydroxycorticosteroids Adrenal Glands - enzymology Animals Cattle Centrifugation, Density Gradient Chemical Precipitation Chromatography, Ion Exchange Deuterium Hydrocortisone Hydrogen Hydrogen-Ion Concentration Kinetics Molecular Weight NAD Oxidoreductases - antagonists & inhibitors Periodic Acid Pregnanes - chemical synthesis Spectrum Analysis Steroids Tritium Ultraviolet Rays
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Zusammenfassung:	An enzyme that catalyzes the reduction of 21-dehydrosteroids has been purified approximately 250-fold from acetone powder extracts of bovine adrenal glands. The reaction is specific for DPNH, but no structural requirements of substrate other than the steroid nucleus were evident. Steroids are competitive inhibitors with respect to 21-dehydrocortisol reduction. The reaction catalyzed was shown to be 21-Dehydrosteroid + DPNH + H + â 21-hydroxysteroid + DPN + The stereospecificity of the hydrogen transfer occurred from the B side of DPNH. Attempts to reverse the reaction have not been successful.
ISSN:	0021-9258 1083-351X
DOI:	10.1016/S0021-9258(19)56971-X