3α-HYDROXYSTEROID DEHYDROGENATION IN SUBCELLULAR FRACTIONS OF RAT VENTRAL PROSTATE AND OTHER TISSUES

Abstract

SUMMARY: Dehydrogenation of androsterone, catalysed by both particulate and soluble fractions of rat ventral prostate, has been demonstrated in vitro by spectrophotometric and chromatographic methods. A difference has been observed between dehydrogenases in the particulate and soluble fractions in their acceptance, under uniform experimental conditions, of the 5α and 5β isomers, androsterone and aetiocholanolone, as substrate. The particulate enzyme dehydrogenates androsterone under conditions in which aetiocholanolone is not dehydrogenated, whereas the soluble enzyme utilizes equally androsterone and aetiocholanolone as substrate. An examination of other rat tissues by the chromatographic method has confirmed the widespread occurrence of the soluble dehydrogenase. Particulate dehydrogenase resembling the prostatic enzyme was detected in seminal vesicle and kidney.