Hostname: page-component-586b7cd67f-g8jcs Total loading time: 0 Render date: 2024-11-29T01:45:56.707Z Has data issue: false hasContentIssue false
  • English
  • Français

Some effects of vitamin E and selenium deprivation on tissue enzyme levels and indices of tissue peroxidation in rainbow trout (Salmo gairdneri)

Published online by Cambridge University Press:  07 March 2008

J. G. Bell ,
C. B. Cowey ,
J. W. Adron  and
Aileen M. Shanks
J. G. Bell
Affiliation:
NERC Institute of Marine Biochemistry, St Fittick's Road, AberdeenABl 3RA
C. B. Cowey
Affiliation:
NERC Institute of Marine Biochemistry, St Fittick's Road, AberdeenABl 3RA
J. W. Adron
Affiliation:
NERC Institute of Marine Biochemistry, St Fittick's Road, AberdeenABl 3RA
Aileen M. Shanks
Affiliation:
Marine Laboratory, Victoria Road, AberdeenAB9 8DB
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. Duplicate groups of rainbow trout (Salrno gairdnert) (mean weight 11 g) were given for 40 weeks one of four partially purified diets that were either adequate or low in selenium or vitamin E or both.

2. Weight gains of trout given the dually deficient diet were significantly lower than those of trout given a complete diet or a diet deficient in Se. No mortalities occurred and the only pathology seen was exudative diathesis in the dually deficient trout.

3. There was significant interaction between the two nutrients both with respect to packed cell volume and to malondialdehyde formation in the in vitro NADPH-dependent microsomal lipid peroxidation system.

4. Tissue levels of vitamin E and Se decreased to very low levels in trout given diets lacking these nutrients. For plasma there was a significant effect of dietary vitamin E on Se concentration.

5. Glutathione (GSH) peroxidase (EC 1. 1 1. 1.9) activity in liver and plasma was significantly lower in trout receiving low dietary Se but was independent of vitamin E intake. The ratios of hepatic GSH peroxidase activity measured with cumene hydroperoxide and hydrogen peroxide were the same for all treatments. This confirms the absence of a Se-independent GSH peroxidase activity in trout liver.

6. Se deficiency did not lead to any compensatory increase in hepatic GSH transferase (EC 2. 5. 1. 18) activity; values were essentially the same in all treatments.

7. Plasma pyruvate kinase (EC 2. 7. 1.40) activity increased significantly in the trout deficient in both nutrients. This was thought to be due to leakage of the enzyme from the muscle and may be indicative of incipient (subclinical) muscle damage.

Type
Papers on General Nutrition
Information
British Journal of Nutrition , Volume 53 , Issue 1 , January 1985 , pp. 149 - 157
Copyright
Copyright © The Nutrition Society 1985

References

REFERENCES

Bell, J. G., Cowey, C. B. & Youngson, A. (1984). Biochimica et Biophysica Acta 795, 91–99.CrossRefGoogle Scholar
Chen, L. H., Chow, C. K. & Thacker, R. R. (1983). Nutrition Reports International 27, 207–212.Google Scholar
Cowey, C. B., Adron, J. W., Walton, M. J., Murray, J., Youngson, A. & Knox, D. (1981). Journal of Nutririon 111, 1556–1567.CrossRefGoogle Scholar
Draper, H. H. & Csallany, A. S. (1969). Journal of nutrition 98, 390–394.CrossRefGoogle Scholar
Duncan, D. B. (1955). Biometrics 11, 1–42.CrossRefGoogle Scholar
Habig, W. H., Pabst, M. J. & Jakoby, W. B. (1974). Journal of biological chemistry 249, 7130–7139.CrossRefGoogle Scholar
Hasunuma, R., Ogawa, T. & Kawanishi, Y. (1982). Analytical Biochemistry 126, 242–245.CrossRefGoogle Scholar
Heisinger, J. F. & Dawson, S. M. (1983). Journal of experimental Zoology 225, 325–327.CrossRefGoogle Scholar
Hilton, J. W., Hodson, P. V. & Slinger, S. J. (1980). Journal of Nutrition 110, 2527–2535.CrossRefGoogle Scholar
Hung, S. S. O., Cho, C. Y. & Slinger, S. J. (1980). Journal of the Association of Official Analytical Chemists 63, 889–893.Google Scholar
Lawrence, R. A., Parkhill, L. K. & Burk, R. F. (1978). Journal of Nutrition 108, 981–987.CrossRefGoogle Scholar
Lowry, O. H., Roseburgh, N. J., Farr, A. L. & Randall, R. J. (1951). Journal of Biological Chemistry 193, 265–275.CrossRefGoogle Scholar
McMurray, C. H., Blanchflower, W. J. & Rice, D. A. (1980). Journal of the Association of Oficial Analytical Chemists 63, 1258–1261.Google Scholar
Oh, S.-H., Sunde, R. A., Pope, A. L. & Hoekstra, W. G. (1976). Journal of Animal Science 42, 977–983.CrossRefGoogle Scholar
Pearse, A. G. E. (1972). Histochemistry, 3rd ed., vol. 2. Edinburgh and London: Churchill Livingstone.Google Scholar
Poston, H. A., Combs, G. F. & Leibovitz, L. (1976). Journal of Nutrition 106, 892–904.CrossRefGoogle Scholar
Schwarz, K. & Folz, C. M. (1957). Journal of the American Chemical society 79, 3293–3298.Google Scholar
Siddons, R. C. & Mills, C. F. (1981). British Journal of Nutrition 46, 345–355.CrossRefGoogle Scholar
Vos, J., Hulstaert, C. E. & Molenaar, I. (1981). Annals of Nutrition and Metabolism 25, 299–306.CrossRefGoogle Scholar