Abstract
Hydrocortisone has been shown to inhibit oxidative metabolism in vitro by liver mitochondria. Results indicate that the primary effect is to increase the permeability of mitochondrial membranes, allowing loss of soluble respiratory cofactors from mitochondrial-enzyme systems. Dehydrogenases dependent on pyridine nucleotides for electron transfer are thus proportionally inactivated. Hydrocortisone is postulated as one of the regulatory factors governing selective semi-permeability of mitochondrial membranes in vivo.