Abstract
1. 1. The activity of phosphogluconate dehydrogenase of a transplanted ethionine-induced hepatoma has been compared with the enzyme of normal liver in the rat. The hepatoma activity is approximately twice that of liver, but a study of the crude and partially-purified enzyme from both sources showed no dissimilarities which might account for this difference. 2. 2. The enzyme in both tissues was localized mainly in the cell sap. Gytochrome oxidase and acid phosphatase were localized in the mitochondrial and lysosomal fractions respectively, although the specific activity of hepatoma tissue was lower than liver.The activities of glucose-6-phosphatase and arylsulphatase C, normally microsomal marker enzymes of liver, were very low and did not exhibit a constant distribution pattern in the hepatoma. 3. 3. The chemical composition and fine structural studies showed that the hepatoma had an altered nucleocytoplasmic ratio and contained less mitochondria per cell than rat liver. In addition, there is a quantitative depletion ofendoplasmic reticulum and an abundance of clusters of free ribosomes in the cytoplasm.
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