» Articles » PMID: 4634827

Dietary Protein Intake and Skeletal-muscle Protein Metabolism in Rats. Studies with Salt-washed Ribosomes and Transfer Factors

Overview
Journal Biochem J
Specialty Biochemistry
Date 1972 Jul 1
PMID 4634827
Citations 2
Authors
Affiliations
Soon will be listed here.
Abstract

1. Aspects of skeletal muscle protein synthesis in vitro were studied in young rats given a low-protein diet for up to 10 days and during re-feeding with an adequate diet. 2. Partially purified muscle transfer factors (transferases I and II), crude and purified (NH(4)Cl-washed) ribosomes and a pH5 enzyme fraction were prepared for this purpose. 3. A marked decrease in the capacity of crude ribosomes to carry out cell-free polypeptide synthesis occurred within 4 days of feeding the low-protein diet. 4. The capacity of salt-washed ribosomes to promote amino acid polymerization, in the presence of added transfer factors and aminoacyl-tRNA, was only slightly decreased by the dietary treatment. 5. However, the capacity of salt-washed ribosomes to bind (14)C-labelled aminoacyl-tRNA was decreased by feeding the low-protein diet. 6. The capacity of the pH5 enzyme fraction to promote amino acid incorporation in a complete cell-free system was decreased within 2 days of feeding the low-protein diet. There is no evidence that the change is associated with aminoacyl-tRNA synthetase or binding enzyme activities of the pH5 fractions. 7. These changes are discussed in relation to the diminished rate of protein synthesis in the intact muscle cell when rats are given a low-protein diet.

Citing Articles

Dietary protein intake and skeletal-muscle protein metabolism in rats. Studies with the ammonium chloride-wash fraction from crude polyribosomes of well-nourished and protein-depleted rats.

Alexis S, Young V Biochem J. 1973; 136(3):773-80.

PMID: 4780699 PMC: 1166014. DOI: 10.1042/bj1360773.


Concentration of elongation factor 2 in rat skeletal muscle during protein depletion and re-feeding.

Alexis S, Young V, Gill D Biochem J. 1974; 142(1):185-8.

PMID: 4374185 PMC: 1168224. DOI: 10.1042/bj1420185.

References
1.
GASIOR E, MOLDAVE K . RESOLUTION OF AMINOACYL-TRANSFERRING ENZYMES FROM RAT LIVER BY MOLECULAR SIEVE CHROMATOGRAPHY. J Biol Chem. 1965; 240:3346-52. View

2.
Young V, Alexis S . In vitro activity of ribosomes and RNA content of skeletal muscle in young rats fed adequate or low protein. J Nutr. 1968; 96(2):255-62. DOI: 10.1093/jn/96.2.255. View

3.
Gaetani S, PAOLUCCI A, Spadoni M, Tomassi G . ACTIVITY OF AMINO ACID-ACTIVATING ENZYMES IN TISSUES FROM PROTEIN-DEPLETED RATS. J Nutr. 1964; 84:173-8. DOI: 10.1093/jn/84.2.173. View

4.
Young V, Chen S, Macdonald J . The sedimentation of rat skeletal-muscle ribosomes. Effect of hydrocortisone, insulin and diet. Biochem J. 1968; 106(4):913-9. PMC: 1198595. DOI: 10.1042/bj1060913. View

5.
Young V, Baliga B, Alexis S, MUNRO H . Lack of in vitro binding of 3-methylhistidine to transfer RNA by aminoacyl ligases from skeletal muscle. Biochim Biophys Acta. 1970; 199(1):297-300. DOI: 10.1016/0005-2787(70)90723-9. View