Hostname: page-component-78c5997874-s2hrs Total loading time: 0 Render date: 2024-11-17T14:51:58.306Z Has data issue: false hasContentIssue false
  • English
  • Français

Methionine metabolism in isolated perfused livers from rats fed on zinc-deficient and restricted diets*

Published online by Cambridge University Press:  09 March 2007

John A. Duerre  and
James C. Wallwork
John A. Duerre
Affiliation:
Department of Microbiology, Ireland Research Laboratory, University of North Dakota, Grand Forks, North Dakota 58202, USA
James C. Wallwork
Affiliation:
United States Department of Agriculture, Agricultural Research Service, Human Nutrition Research Center, Grand Forks, North Dakota, 58202, USA
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. Sulphur amino acid metabolism in livers from rats which had been fed ad lib. on a restricted diet (malnourished) or a Zn-deficient diet was investigated. Perfusion of normal livers with different amounts of L-methionine revealed that homocysteine was recycled four to five times before being eliminated via the transsulphuration pathway.

2. From the perfusion experiments, we found no evidence that any of the enzymes involved in recycling homocysteine back to methionine (methylation pathway) were adversely effected by Zn deficiency or malnutrition.

3. The intracellular concentration of cystathionine and S-adenosylmethionine increased in all livers in response to increased concentrations of L-methionine (L-Met) in the perfusate.

4. The intracellular concentration of S-adenosylhomocysteine remained the same in all livers regardless of the concentration of perfusate methionine.

5. Although homocysteine did not accumulate in the cell, it was excreted into the perfusate. The amount of homocysteine in the perfusate of livers from Zn-deficient rats was higher than either ad lib. or pair-fed rats.

6. The breakdown of homocysteine, via the transsulphuration pathway, was augmented by Zn deficiency. This was apparent from the greater amount of α-ketobutyrate excreted by livers from Zn-deficient rats compared with pair-fed or ad lib.-fed controls.

7. The increase in metabolism of L-Met, via the transsulphuration pathway, in the livers from Zn-deficient rats appears to reflect the lack of demand for this compound in protein synthesis and methylation reactions (Wallwork & Duerre, 1985).

Type
Papers on General Nutrition
Information
British Journal of Nutrition , Volume 56 , Issue 2 , September 1986 , pp. 395 - 405
Copyright
Copyright © The Nutrition Society 1986

References

REFERENCES

Cohen, P. O. (1959). In Manometric Techniques, pp. 135–169 [Umbreit, W. W., Burris, R. H. and Stauffer, J. F., editors]. New York: Burgess Publishing Co.Google Scholar
Coward, J. K., D'Urso-Scott, M. & Sweet, W. O. (1972). Biochemical Pharmacology 21, 1200–1203.CrossRefGoogle Scholar
Dancis, J., Hutzler, J. & Levitz, M. (1963). Biochimica Biophysica Acta 78, 85–90.CrossRefGoogle Scholar
Deguchi, T. & Barchas, J. (1971). Journal of Biological Chemistry 246, 3175–3181.CrossRefGoogle Scholar
de la Haba, G. & Cantoni, G. L. (1959). Journal of Biological Chemistry 234, 603–608.CrossRefGoogle Scholar
Duerre, J. A. (1968). Archives of Biochemistry and Biophysics 124, 422–430.CrossRefGoogle Scholar
Duerre, J. A., Ford, K. M. & Sandstead, H. H. (1977). Journal of Nutrition 107, 1082–1093.CrossRefGoogle Scholar
Finkelstein, J. D., Kyle, W. E. & Harris, B. J. (1974). Archives of Biochemistry and Biophysics 165, 774–779.CrossRefGoogle Scholar
Fosmire, G. J. & Sandstead, H. H. (1977). Proceedings of the Society for Experimental Biology and Medicine 154, 351–355.CrossRefGoogle Scholar
Friedemann, T. E. & Haugen, G. E. (1943). Journal of Biological Chemistry 147, 415–442.CrossRefGoogle Scholar
Hoffman, D. R., Marion, D. W., Cornatzer, W. E. & Duerre, J. A. (1980). Journal of Biological Chemistry 255, 10822–10827.CrossRefGoogle Scholar
Hsu, J. M., & Anthony, W. L. (1970). Journal of Nutrition 100, 1189–1196.CrossRefGoogle Scholar
Hsu, J. M., Anthony, W. L. & Buchanan, P. J. (1969). Journal of Nutrition 99, 425–432.CrossRefGoogle Scholar
Jacob, F. A. & Crandall, J. C. (1972). Nutrition Reports International 5, 27–36.Google Scholar
McKenzie, J. M., Fosmire, G. J. & Sandstead, H. H. (1975). Journal of Nutrition 105, 1466–1476.CrossRefGoogle Scholar
Mudd, S. H., & Poole, J. R. (1975). Metabolism, Clinical and Experimental 24, 721–735.CrossRefGoogle Scholar
Sandstead, H. H. & Rinaldi, R. A. (1969). Journal of Cellular Physiology 73, 81–84.CrossRefGoogle Scholar
Schatz, R. A., Vunnam, C. R. & Sellinger, O. Z. (1979). In Transmethylation, pp. 143–153 [Usdin, E., Borchardt, R. T. and Creveling, C. R., editors]. New York: Elsevier North Holland.Google Scholar
Scheffé, H. (1959). The Analysis of Variance, pp. 90–137. New York: John Wiley.Google Scholar
Veneziale, C. M., Walter, P., Kneer, N. & Lardy, H. A. (1967). Biochemistry 6, 2129–2138.CrossRefGoogle Scholar
Walker, R. D. & Duerre, J. A. (1975). Canadian Journal of Biochemistry 53, 312–319.CrossRefGoogle Scholar
Wallwork, J. C. & Duerre, J. A. (1985). Journal of Nutrition 115, 252–262.CrossRefGoogle Scholar
Wallwork, J. C., Fosmire, G. J. & Sordstead, H. H. (1981). British Journal of Nutrition 45, 127–136.CrossRefGoogle Scholar
Wallwork, J. C., Leland, S. A. & Duerre, J. A. (1986). Proceedings of the Fifth International Symposium on Trace Element Metabolism in Man and Animals, vol. 5. (In the Press).Google Scholar
Williams, R. B. & Chesters, J. K. (1970). British Journal of Nutrition 24, 1053–1059.CrossRefGoogle Scholar
Zappia, V., Zydek-Cwick, C. R. & Schlenk, F. (1969). Journal of Biological Chemistry 244, 4499–4509.CrossRefGoogle Scholar