Proteolytic degradation of histones and site of cleavage in histone F2al and F3.
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Biomedical subjects
Publications and source records attributed to C Von Holt.
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The overall oxidative degradation of leucine and phenylalanine, measured in vivo in rats fed on a 2%-casein diet for 8 weeks, is markedly decreased as compared with controls, whereas that of glutamate and alanine is apparently unaffected. The decrease in leucine degradation is due, at least in part, to a block before the formation of 3-methylbutyryl-CoA (isovaleryl-CoA) in the catabolic pathway. This phenomenon is accompanied by increased incorporation of [(14)C]leucine into liver proteins, decreased urinary excretion of leucine and increased urinary excretion of 4-methyl-2-oxopentanoate (alpha-oxoisocaproate) by protein-depleted animals. The results suggest the existence of adaptive mechanisms that function to conserve an indispensable carbon skeleton.
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.
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