Hostname: page-component-586b7cd67f-rcrh6 Total loading time: 0 Render date: 2024-11-29T18:25:49.305Z Has data issue: false hasContentIssue false

Protein synthesis in muscle of mature sheep

Published online by Cambridge University Press:  27 March 2009

D. T. W. Bryant
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading, RG2 9AT
R. W. Smith
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading, RG2 9AT

Summary

Protein synthesis was measured in wether sheep by constant intravenous infusion of [3H]tyrosine. The specific radioactivity of plasma tyrosine at plateau was used to calculate tyrosine flux and the rate of protein synthesis in the whole body was estimated. For wethers fed hay and concentrates tyrosine flux was 2·46 mmol/h and protein synthesized was 5·29 g/kg body weight per day. Corresponding values for wethers fed barley straw were 30–35% lower.

Fractional rates of protein synthesis in individual muscles were between 2 and 3% per day for diaphragm, longissimus dorsi, gastrocnemius, semitendinosus and vastus lateralis muscles from wethers fed hay and concentrates, but the value for vastus intermedius was higher. Corresponding rates for wethers fed barley straw were 18–36% lower.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1982

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Adamson, L. F., Herington, A. C. & Bornstein, J. (1972). Evidence for the selection by the membrane transport system of intracellular or extracellular amino acids for protein synthesis. Biochimica et Biophysica Acta 282, 352365.CrossRefGoogle ScholarPubMed
Arnal, M. (1977). Muscle protein turnover in lambs throughout development. Proceedings of the 2nd International Symposium on Protein Metabolism and Nutrition, Lelystad, The Netherlands, pp. 3537.Google Scholar
Block, R. J. & Weiss, K. W. (1956). Amino Acid Handbook, p. 344. Springfield, Illinois: Thomas.Google Scholar
Buttery, P. J., Beckerton, A., Mitchell, K. M., Davies, K. & Annison, E. F. (1975). The turnover rate of muscle and liver protein in sheep. Proceedings of the Nutrition Society 34, 91A92A.Google ScholarPubMed
Fern, E. B. & Garlick, P. J. (1974). The specific radioactivity of the tissue free amino acid pool as a basis for measuring the rate of protein synthesis in the rat in vivo. Biochemical Journal 142, 413419.CrossRefGoogle Scholar
Gan, J. C. & Jeffay, H. (1967). Origins and metabolism in the intracellular amino acid pools in rat liver and muscle. Biochimica el Biophysica Acta 148, 448459.CrossRefGoogle ScholarPubMed
Garlick, P. J., Burk, T. L. & Swick, R. W. (1976). Protein synthesis and RNA in tissues of the pig. American Journal of Physiology 230, 11081112.CrossRefGoogle ScholarPubMed
Garlick, P. J. & Marshall, I. (1972). A technique for measuring brain protein synthesis. Journal of Neurochemistry 19, 577583.CrossRefGoogle ScholarPubMed
Garlick, P. J., Millward, D. J. & James, W. P. T. (1973). The diurnal response of muscle and liver protein synthesis in vivoin meal-fed rats. Biochemical Journal 136, 935945.CrossRefGoogle Scholar
Garlick, P. J., Millward, D. J., James, W. P. T. & Waterlow, J. C. (1975). The effect of protein deprivation and starvation on the rate of protein synthesis in tissues of the rat. Biochimica et Biophysica Acta 414, 7184.CrossRefGoogle ScholarPubMed
Hider, R. C., Fern, E. B. & London, D. R. (1971). Identification in skeletal muscle of a distinct extracellular pool of amino acids, and its role in protein synthesis. Biochemical Journal 121, 817827.CrossRefGoogle ScholarPubMed
James, W. P. T., Garlick, P. J., Sender, P. M. & Waterlow, J. C. (1976). Studies of amino acid and protein metabolism in normal man with L-[U-14C]-tyrosine. Clinical Science and Molecular Medicine 50, 525532.Google Scholar
Lobley, G. E., Milne, V., Lovie, J. M., Reeds, P. J. & Pennis, K. (1980). Whole body and tissue protein synthesis in cattle. British Journal of Nutrition 43, 491502.CrossRefGoogle ScholarPubMed
Millward, D. J. (1970). Protein turnover in skeletal muscle. II. The effect of starvation and a protein free diet on the synthesis and catabolism of skeletal muscle proteins in comparison to liver. Clinical Science 39, 591603.CrossRefGoogle Scholar
Millward, D. J., Garlick, P. J., Nnanyelugo, D. O. & Waterlow, J. C. (1976). The relative importance of muscle protein synthesis and breakdown in the regulation of muscle mass. Biochemical Journal 156, 185188.CrossRefGoogle ScholarPubMed
Millward, D. J., Garlick, P. J., Stewart, R. J. C., Nnanyelugo, D. O. & Waterlow, J. C. (1975). Skeletal muscle growth and protein turnover. Biochemical Journal 150, 235243.CrossRefGoogle ScholarPubMed
Reeds, P. J., Cadenhead, A., Fuller, M. F., Lobley, G. E. & McDonald, J. D. (1980). Protein turnover in growing pigs. Effects of age and food intake. British Journal of Nutrition 43, 445455.CrossRefGoogle ScholarPubMed
Reeds, P. J. & Lobley, G. E. (1980). Protein synthesis are there real species differences? Proceedings of the Nutrition Society 39, 4352.CrossRefGoogle ScholarPubMed
Simon, O., Münchmeyer, R., Berger, H., Zebrowska, T. & Buraczewska, L. (1978). Estimation of rate of protein synthesis by constant infusion of labelled amino acids in pigs. British Journal of Nutrition 40, 243252.CrossRefGoogle ScholarPubMed
SoltÉsz, G., Joyce, J. & Young, M. (1973). Protein synthesis rate in the newborn lamb. Biology of the Neonate 23, 139148.CrossRefGoogle ScholarPubMed
Thompson, J. F., Morris, C. J. & Gering, R. K. (1959). Purification of plant amino acids for paper chromatography. Analytical Chemistry 31, 10281031.CrossRefGoogle Scholar