Abstract
Summary
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.
Supported by funds from the National Heart and Lung Institute of U.S. Public Health Service (R01 HL 13205). The authors thank Mrs. Lillie Bell for her technical assistance and Mrs. Hedy Boelte for her secretarial assistance.
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