Abstract
In vitro experiments with rat hepatic glucose-6-phosphate dehydrogenase have shown that the activity of this enzyme is significantly inhibited by dehydroepiandro-sterone, androstenedione, androsterone and etiocholanolone at concentrations of 10-4 and 5×10-4 M. At these concentrations, dehydroepiandrosterone has specific inhibitory effects on glucose-6-phosphate dehydrogenase isoenzymes separated by acrylamide gel electrophoresis.