Source of amino acids for tRNA acylation in growing chicks
- 1 January 1994
- journal article
- Published by Springer Nature in Amino Acids
- Vol. 7 (3) , 267-278
- https://doi.org/10.1007/bf00807702
Abstract
Specific radioactivity in three amino acid compartments was examined in broiler chicks following a flooding dose of leucine or phenylalanine. In general, specific radioactivity of leucine and phenylalanine in deproteinated plasma (SAe) and tissue (SAi) compartments, exceeded that in acylated-tRNA (SAt). In most tissues, SAe and SAi rapidly reached a similar peak level by 5 min followed by a slow decline for the next 30 minutes. Many tissues (eg. GI tract, liver, skin, and thigh) failed to maintain equilibrium between SAe and SAi over time. More metabolically active tissues, such as GI and liver had the greatest differences between these compartments. The difference between SAe and SAi for both leucine and phenylalanine were due to SAi decreasing faster than SAe, indicating dilution with unlabelled amino acids from proteolysis. Plasma and tissue specific radioactivity overestimated tRNA specific radioactivity by as much as 5 and 2.8 fold using leucine or 2.7 and 1.4 fold using phenylalanine, respectively. These data suggest that intracellular compartmentation of protein metabolism and the coupling of protein degradation and synthesis occur, in vivo.Keywords
This publication has 34 references indexed in Scilit:
- Amino acid flooding doses for measuring rates of protein synthesisAmino Acids, 1993
- Determination of Regional Rates of Cerebral Protein Synthesis Adjusted for Regional Differences in Recycling of Leucine Derived from Protein Degradation into the Precursor Pool in Conscious Adult RatsJournal of Neurochemistry, 1992
- Effect of Loading Doses of l‐Valine on Relative Contributions of Valine Derived from Protein Degradation and Plasma to the Precursor Pool for Protein Synthesis in Rat BrainJournal of Neurochemistry, 1991
- Channeling of aminoacyl-tRNA for protein synthesis in vivo.Proceedings of the National Academy of Sciences, 1991
- Parathyroid hormone alteration of free and tRNA-bound proline specific activities in cultured mouse osteoblast-like cellsBiochemical and Biophysical Research Communications, 1989
- Association of an aminoacyl-tRNA synthetase complex and of phenylalanyl-tRNA synthetase with the cytoskeletal framework fraction from mammalian cellsExperimental Cell Research, 1985
- Rapid analysis of amino acids using pre-column derivatizationJournal of Chromatography B: Biomedical Sciences and Applications, 1984
- Protein synthesis rates in rat muscle and skin based on lysyl-tRNA radioactivityJournal of Surgical Research, 1983
- Protein synthesis in pulmonary alveolar macrophages Source of amino acids for leucyl-tRNABiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1981
- Amino acid inhibition of the autophagic/lysosomal pathway of protein degradation in isolated rat hepatocytesBiochimica et Biophysica Acta (BBA) - General Subjects, 1980