title: Metabolism of leucine in protein-calorie-deficient rats.
abstract: 1. Protein-calorie-depleted rats exhibit a decreased ability to oxidize leucine as compared with control animals. 2. The block in degradation of l-leucine is due to decreased activities of l-leucine transaminase and d-amino acid oxidase associated with liver mitochondria. 3. Cytoplasmic l-leucine transaminase in liver is not affected by the protein depletion. 4. The specific activities of the mitochondrial enzymes can be increased by a single oral dose of 1g. of Bacto-Peptone (meat hydrolysate). The effect of Bacto-Peptone can be inhibited by prior administration of dosages of 10mg. of puromycin/100g. body wt., suggesting that the increased enzyme specific activities may be due to new synthesis of enzyme protein.
mesh_terms: D000818:Animals; D003593:Cytoplasm / Q000201:enzymology; D003605:D-Amino-Acid Oxidase / Q000096:biosynthesis / Q000378:metabolism; D003677:Deficiency Diseases / Q000378:metabolism*; D003864:Depression, Chemical; D007930:Leucine / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D008930:Mitochondria, Liver / Q000201:enzymology; D010084:Oxidation-Reduction; D011488:Protein Deficiency / Q000378:metabolism*; D011492:Protein Hydrolysates / Q000378:metabolism; D011691:Puromycin / Q000494:pharmacology; D051381:Rats; D000637:Transaminases / Q000096:biosynthesis / Q000378:metabolism
chemical_list: D011492:Protein Hydrolysates; D011691:Puromycin; D003605:D-Amino-Acid Oxidase; D000637:Transaminases; D007930:Leucine