Hostname: page-component-cd9895bd7-dk4vv Total loading time: 0 Render date: 2024-12-26T13:13:40.678Z Has data issue: false hasContentIssue false
  • English
  • Français

Protein turnover in rats treated with Trienbolone acetate

Published online by Cambridge University Press:  09 March 2007

Briman G. Vernon  and
Peter J. Buttery
Briman G. Vernon
Affiliation:
Department of Applied Biochemistry & Nutrition, University of Nottingham School of Agriculture, Sutton Bonington, Loughborough, Leics
Peter J. Buttery
Affiliation:
Department of Applied Biochemistry & Nutrition, University of Nottingham School of Agriculture, Sutton Bonington, Loughborough, Leics
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

1. The anabolic agent Trienbolone acetate (3-oxo-17-β-hydroxy-4,9,11-estratriene acetate) given subcutaneously to female rats increased their growth rate compared with untreated controls (P < 0.001).

2. The compound had little androgenic activity.

3. The fractional synthetic and fractional degradative rates of the mixed muscle proteins were smaller in the treated rats than in the control rats.

Type
Short Papers
Information
British Journal of Nutrition , Volume 36 , Issue 3 , November 1976 , pp. 575 - 579
Copyright
Copyright © The Nutrition Society 1976

References

Barragry, T. B. (1974). Ir. Vet. J. 28, 28.Google Scholar
Best, J. M. J. (1972). Vet. Rec. 91, 624.CrossRefGoogle Scholar
Buttery, P. J. & Annison, E. F. (1973). In The Biological Efficiency of Protein Production, p. 141 [Jones, J. W. G. editor]. London: Cambridge University Press.Google Scholar
Chan, K. H., Heitzman, R. J. & Kitchenham, B. A. (1975). Br. Vet. J. 131, 170.CrossRefGoogle Scholar
Florini, J. R. & Breuer, C. B. (1965). Biochemistry, 4, 1544.CrossRefGoogle Scholar
Garlick, P. J. & Marshall, I. (1972). J. Neurochem. 19, 579.CrossRefGoogle Scholar
Garlick, P. J., Burke, T. L. & Swick, R. T. (1976). Am. J. Phys. 230, 1108.Google Scholar
Grandadam, J. A., Schield, J. P., Jobard, A., Dreux, H. & Boisson, J. M. (1975). J. Anim. Sci. 41, 969.CrossRefGoogle Scholar
Herschberger, L. G., Shipley, E. G. & Meyer, R. K. (1953). Proc. Soc. exp. Biol. Med. 83, 175.CrossRefGoogle Scholar
Heitzman, R. J. & Chan, K. H. (1974). Br. Vet. J. 130, 532.CrossRefGoogle Scholar
Jelinek, J., Vesela, H. & Valova, B. (1964). Acta endocr. Copnh. 46, 352.Google Scholar
Jensen, E. V. & DeSombre, E. R. (1972). Ann. Rev. Biochem. 41, 203.CrossRefGoogle Scholar
Lobl, R. T. & Maenza, R. M. (1975). Biol. Reprod. 13, 255.Google Scholar
Millward, D. J. (1970). Clin. Sci. 39, 577.CrossRefGoogle Scholar
Millward, D. J., Garlick, P. J., Nnanyelugo, D. O. & Waterlow, J. C. (1976). Biochem. J. 156, 185.CrossRefGoogle Scholar
Waalkes, T. P. & Udenfriend, S. (1957). J. Lab. Clin. Med. 50, 733.Google Scholar
Waterlow, J. C. & Stephen, J. M. L. (1967). Clin. Sci. 33, 489.Google Scholar
Waterlow, J. C. & Stephen, J. M. L. (1968). Clin. Sci. 35, 287.Google Scholar