Studies on triiodothyronine-induced synthesis of liver mitochondrial alpha-glycerophosphate dehydrogenase in the thyroidectomized rat.

摘要: Administration of a single small dose triiodothymonine (T3) greatly increased liver mitochondrial L-α-glycerophosphate dehydrogenase activity thyroidectomized rats. The induction L-α-glycerophoshate by T3 could be blocked simultaneous administration puromycin; in addition, time incorporation L-leucine-14C into total proteins and all subcellular fractions was inhibited. Furthermore, puromycin further when it administered after the T3. L-Ethionine prevented enzyme formation, inhibition partially reversed L-methionine. "Pulse labeling" used to study proteins, data indicate that an rate protein synthesis precedes maximal increase produced T3-administration. These observations suggest T3-induction rat results from acceleration synthesis. Similar were reported earlier with euthyroid rat. actinomycin D along abolished mitochondria. also inhibited 5-fluorouracil. process depends on formation adequate amount renewable messenger-RNA molecules.