Abstract
Deposition of ubiquinone and preferably of a crude phospholipid mixture and ubiquinone on cryostat sections of mouse kidney, liver and heart increased the intensity of staining for succinic dehydrogenase. A similar treatment partly restored the activity of this enzyme which was reduced by exposure to 60°C, long storage at 37°C, oxidation and treatment with lipid solvents. The restoration was present only in the case of mild noxious treatments. It is suggested that removal or structural alteration of ubiquinone and phospholipids may limit the rate of dehydrogenase activity; more drastic treatments affect the enzyme itself so that these factors cannot exert any restorative activity.

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