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The influence of the nutritive value of proteins on the level of protein synthesis in vitro in rat skeletal muscle

Published online by Cambridge University Press:  09 March 2007

P. T. Omstedt  and
Alexandra Von Der Decken
P. T. Omstedt
Affiliation:
The Wenner-Gren Institute for Experimental Biology, Stockholm, Sweden
Alexandra Von Der Decken
Affiliation:
The Wenner-Gren Institute for Experimental Biology, Stockholm, Sweden
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Abstract

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1. The amino acid incorporating activity of skeletal muscle ribosomes was studied in rats under various nutritional conditions using labelled amino acids.

2. Ribosomes were obtained from rats that were given a protein-free diet for 5 d followed by a high-protein diet containing casein, gelatin or wheat gluten for 16.5 h and from others that were given one of these protein-containing diets or one containing protein from polished rice for 6 d.

3. The level of isotope incorporation relative to RNA was somewhat higher when the protein source given for 16.5 h was a good-quality protein such as casein than with gelatin or wheat gluten, but fine discrimination between proteins was not considered to be feasible with this system.

4. In the rats that were given the protein-containing diets for 6 d the differences were more pronounced and the amino acid incorporating activity was correlated with the biological value of the protein.

Type
General Nutrition
Information
British Journal of Nutrition , Volume 27 , Issue 3 , May 1972 , pp. 467 - 474
Copyright
Copyright © The Nutrition Society 1972

References

Enwonwu, C. O. & Munro, H. N. (1970). Archs Biochem. Biophys. 138, 532.CrossRefGoogle Scholar
FAO (1970). F.A.O. nutv. Stud. no. 24.Google Scholar
Kaplan, J. H. & Pitot, H. C. (1970). In Mammalian Protein Metabolism Vol. 4, p. 387 [Munro, H. N., editor]New York and London: Academic Press.CrossRefGoogle Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). J. biol. Chem. 193, 265.CrossRefGoogle Scholar
Mans, R. J. & Novelli, G. D. (1961). Archs Biochem. Biophys. 94, 48.CrossRefGoogle Scholar
Munro, H. N. (1968). Fedn Proc. Fedn Am. Socs exp. Biol. 27, 1231.Google Scholar
Ogur, M. & Rosen, G. (1950). Archs Biochem. 25, 262.Google Scholar
Peters, R. F., Richardson, M. C., Small, M. & White, A. M. (1970). Biochem. J. 116, 349.CrossRefGoogle Scholar
Shafritz, D. A., Prichard, P. M., Gilbert, J. M. & Anderson, W. F. (1970). Biochem. biophys. Ref. Commun. 38, 721.CrossRefGoogle Scholar
von der Decken, A. (1967). J. Cell Biol. 33, 657.CrossRefGoogle Scholar
von der Decken, A. (1968 a). Eur. J. Biochem. 4, 87.CrossRefGoogle Scholar
von der Decken, A. (1968 b). Abh. dt. Akad. Wiss. Berl, 1, 541.Google Scholar
von der Decken, A. (1969 a). J. Cell Biol. 43. 138.CrossRefGoogle Scholar
von der Decken, A. (1969 b). In Protein Biosynthesis p. 33 [P., Szafranski, S., Klita and P., Maslowski, editors]. Warszawa: Polish Biochemical Society.Google Scholar
von der Decken, A. & Omstedt, P. T. (1970). J. Nutr. 100, 623.CrossRefGoogle Scholar
Waterlow, J. C. (1969). In Mmnmalian Protein Metabolism Vol. 3, p. 326 [Munro, H. N., editor]. New York and London: Academic Press.Google Scholar
Waterlow, J. C. & Stephen, J. M. L. (1968). Clin. Sci. 35, 287.Google Scholar