Hostname: page-component-76fb5796d-25wd4 Total loading time: 0 Render date: 2024-04-26T10:24:37.064Z Has data issue: false hasContentIssue false
  • English
  • Français

Changes in body-weight, composition and hepatic enzyme activities in response to dietary methionine, betaine and choline levels in growing chicks

Published online by Cambridge University Press:  09 March 2007

C. Linda Saunderson  and
James Mackinlay
C. Linda Saunderson
Affiliation:
AFRC Institute for Grassland and Animal Production, Poultry Department, Roslin, Midlothian EH25 9PS
James Mackinlay
Affiliation:
AFRC Institute for Grassland and Animal Production, Poultry Department, Roslin, Midlothian EH25 9PS
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.

The experiments described here were set up (a) to investigate the effect of age and (b) to investigate the effect of giving five diets which varied in methionine and choline or betaine contents on some of the enzymes that metabolize these nutrients in chick liver. Growth and carcass composition of the chicks fed on the different diets were also examined. There was no obvious relationship between age and enzyme activity in young chicks. Only a diet low in methionine (but not one low in choline) showed a significant decrease in growth and a change in carcass composition. The effects of diet on enzyme activity were complex. Choline oxidase (EC 1.1.3.17) activity was affected by the level of choline in the diet, being high when choline was present at high levels, especially when methionine was limiting. 5-Methyl-tetrahydrofolate homocysteine methyltransferase (EC 2.1.1.3) had a high activity in the livers of chicks fed on a conventional diet compared with those given semi-purified diets. Other enzymes showed minor changes in response to the diet. The diet low in methionine showed a lower activity of cystathionine η-synthase (EC 4.2.1.22) and slightly higher activities of methionine adenosyltransferase (EC 2.5.1.6) and betaine–homocysteine methyltransferase (EC 2.1.1.5; compared with other diets), suggesting that this diet encouraged re-methylation of homocysteine at the expense of trans-sulphuration to cystathionine. The findings obtained in these studies form a useful basis for further investigation of the metabolic interrelationships between methionine and related nutrients.

Keywords

MethionineCholineBetaineChickens
Type
Vitamins
Information
British Journal of Nutrition , Volume 63 , Issue 2 , March 1990 , pp. 339 - 349
Copyright
Copyright © The Nutrition Society 1990

References

Blair, J. C., Harber, C. D., McNab, J. M., Mitchell, G. G. & Scougall, R. K. (1981). Analytical Data of Poultry Feedstuffs, 1977–1980. Occasional Publication no. 1. Roslin, Midlothian: ARC Poultry Research Centre.Google Scholar
Bolton, W. & Blair, R. (1974). Poultry Nutrition, Bulletin no. 174, 4th ed. London: H.M. Stationery Office.Google Scholar
Bryan, L. (1985). Protein deposition in poultry. PhD Thesis, University of Nottingham.Google Scholar
Fau, D., Bois-Joyeux, B., Delhomme, B., Chanez, M. & Peret, J. (1980). Long term effects of methionine excess on rat metabolism. Nutrition Reports International 21, 577–585.Google Scholar
Finkelstein, J. D. (1967). Methionine metabolism in mammals: effects of age, diet and hormones on three enzymes of the pathway in rat tissues. Archives of Biochemistry and Biophysics 122, 583–590.CrossRefGoogle Scholar
Finkelstein, J. D., Kyle, W. E. & Harris, B. J. (1971). Methionine metabolism in mammals: regulation of homocysteine methyltransferase in rat tissues. Archives of Biochemistry and Biophysics 146, 84–92.CrossRefGoogle Scholar
Finkelstein, J. D. & Martin, J. J. (1984). Methionine metabolism in mammals: distribution of homocysteine between competing pathways. Journal of Biological Chemistry 259, 9508–9513.CrossRefGoogle ScholarPubMed
Finkelstein, J. D. & Martin, J. J. (1986). Methionine metabolism in mammals: adaptation to methionine excess. Journal of Biological Chemistry 261, 1582–1587.CrossRefGoogle ScholarPubMed
Finkelstein, J. D., Martin, J. J., Harris, B. J. & Kyle, W. E. (1983). Regulation of hepatic betaine homocysteine methyltransferase by dietary betaine. Journal of Nutrition 113, 519–521.CrossRefGoogle ScholarPubMed
Finkelstein, J. D. & Mudd, S. H. (1967). Transsulfuration in mammals: methionine sparing effects of cystine. Journal of Biological Chemistry 242, 873–880.CrossRefGoogle ScholarPubMed
Girard-Globa, A., Robin, P. & Forestier, M. (1972). Long term adaptation of weaning rats to high dietary levels of methionine and serine. Journal of Nutrition 102, 209–218.CrossRefGoogle Scholar
Keshavarz, K. & Fuller, H. L. (1971). Relationship of arginine and methionine to creatine formation in chicks. Journal of Nutrition 101, 855–862.CrossRefGoogle ScholarPubMed
Kotb, M. & Kredich, N. M. (1985). S-adenosyl methionine synthetase from human lymphocytes. Journal of Biological Chemistry 260, 3923–3930.CrossRefGoogle ScholarPubMed
Lowry, K. R., Izquierdo, O. A. & Baker, D. H. (1987). Efficacy of betaine relative to choline as a methyl donor. Poultry Science 66, Suppl. 1, 135.Google Scholar
McMinn, C. L. & Ottaway, J. H. (1976). On the control of enzyme pathways. Journal of Theoretical Biology 56, 57–73.CrossRefGoogle ScholarPubMed
Mudd, S. H., Finkelstein, J. D., Irreverre, F. & Laster, L. (1965). Transsulfuration in mammals: microassays and tissue distributions of three enzymes in the pathway. Journal of Biological Chemistry 240, 4382–4392.CrossRefGoogle ScholarPubMed
Mudd, S. H., Levy, H. L. & Morrow, G. (1970). Deranged B12 metabolism: Effects on sulfur amino acid metabolism. Biochemical Medicine 4, 193–214.CrossRefGoogle Scholar
Ottaway, J. H. (1979). Simulation of metabolic events. In Techniques in Metabolic Research B219, pp. 1–27 [Kornberg, H. L., Metcalfe, J. C., Northcote, D. H., Pogson, C. I. and Tipton, K. F., editors]. Amsterdam: Elsevier/ North Holland Scientific Publishers.Google Scholar
Percival, G. S., Dunn, S. H., Howe, J. M. & Clark, H. E. (1970). Interaction between methionine, fat and choline in the growing rat. Journal of Nutrition 100, 664–670.CrossRefGoogle Scholar
Pesti, G. M., Harper, A. E. & Sunde, M. L. (1980). Choline/methionine nutrition of starting broiler chicks. Three models for estimating the choline requirement with economic considerations. Poultry Science 59, 1073–1081.CrossRefGoogle ScholarPubMed
Radcliffe, B. C. & Egan, A. R. (1974). A survey of methionine adenosyltransferase and cystathionine γ-lyase activities in ruminant tissues. Australian Journal of Biological Science 27, 465–471.CrossRefGoogle ScholarPubMed
Saunderson, C. L. & Leslie, S. (1988). Muscle growth and protein degradation during early development in chicks of fast and slow growing strains. Comparative Biochemistry and Physiology 89A, 333–337.CrossRefGoogle Scholar
Saunderson, C. L. & Leslie, S. (1989). Cathepsin B, D and H activities in muscles of chicks of fast and slow growing strains: effect of age and diet. Comparative Biochemistry and Physiology 92A, 305–311.CrossRefGoogle Scholar
Selim, A. S. M. & Greenberg, D. M. (1959). An enzyme that synthesises cystathionine and deaminates L-serine. Journal of Biological Chemistry 234, 1474–1480.CrossRefGoogle ScholarPubMed
Skiba, W. E., Taylor, M. P., Wells, M. S., Magnum, J. H. & Awad, W. M. (1982). Human hepatic methionine biosynthesis: Purification and characterisation of betaine homocysteine S-methyltransferase. Journal of Biological Chemistry 257, 14944–14948.CrossRefGoogle ScholarPubMed
Xue, G.-P. & Snoswell, A. M. (1985). Comparative studies on the methionine synthesis in sheep and rat tissues. Comparative Biochemistry and Physiology 80B, 489–494.Google Scholar
Xue, G.-P. & Snoswell, A. M. (1986). Developmental changes in the activities of enzymes related to methyl group metabolism in sheep tissues. Comparative Biochemistry and Physiology 83B, 115–120.Google Scholar
Zeisel, S. H. & Wurtman, R. J. (1981). Developmental changes in rat blood choline concentration. Biochemical Journal 198, 565–570.CrossRefGoogle ScholarPubMed