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( National Cancer Institute, National Institutes of Health, U.S. Public Health Service, Federal Security Agency, Bethesda, Md.)
It has been shown that an active mechanism for oxidative phosphorylation exists in mitochondria of transplantable mouse hepatoma. Large amounts of inorganic phosphate were taken up with the formation of ATP during the oxidation of a-ketoglutarate, glutamate, and succinate. The phosphorylation system in tumor exhibited more lability than that in liver and showed a more definite requirement for DPN in the case of those substrates the oxidation of which requires this cofactor. P:O ratios were determined for the oxidation of a-ketoglutarate and succinate by tumor and liver mitochondria, but no significant differences due to tissue were observed. The specific activities of ketoglutaric and succinic oxidases were determined under the conditions of active phosphorylation. The specific phosphorylating activities associated with ketoglutarate, glutamate, and succinate oxidations in tumor mitochondria were also determined and compared to those of liver mitochondria. The specific ketoglutaric oxidase activity and the corresponding phosphorylating activity of tumor mitochondria were very nearly equal to those of liver mitochondria, but, in the case of succinate, both activities were less for tumor mitochondria.
Received 10/ 8/51.
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