Hostname: page-component-76fb5796d-wq484 Total loading time: 0 Render date: 2024-04-26T09:16:26.062Z Has data issue: false hasContentIssue false

The effect of dietary bagasse on the activities of some key enzymes of carbohydrate and lipid metabolism in mouse liver

Published online by Cambridge University Press:  09 March 2007

John C. Stanley
Affiliation:
Department of Biochemistry, University of Oxford, South Parks Road, OxfordOX1 3QU
Eric A. Newsholme
Affiliation:
Department of Biochemistry, University of Oxford, South Parks Road, OxfordOX1 3QU
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 effects of a 100 g/kg diet substitution of bagasse on the body-weight gain, food consumption and faecal dry weight of mice given a high-sucrose diet and on the activities of hepatic glucose-6-phosphate dehydrogenase (EC 1. 1. 1. 49), 6-phosphogluconate dehydrogenase (EC I. I. I. 44), malate dehydrogenase (oxaloacetatedecarboxylating) (NADP+) (EC I. I. I. 40), ATP-citrate (pro-3S) lyase (EC 4. 1. 3.8), 6-phosphofructokinase (EC 2. 7. 1. II), pyruvate kinase (EC 2.7. 1. 40) and fructose-1,6-bisphosphatase (EC 3. 1. 3. II) were studied.

2. Bagasse had no effect on body-weight gain, food consumption or faecal dry weight.

3. Bagasse decreased the activities of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and phosphofructokinase expressed on a wet weight basis and on a protein basis.

4. Bagasse decreased the activities of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydro-genase expressed on a body-weight basis.

5. These results suggest that bagasse decreases the flux through some pathways of hepatic lipogenesis when mice are given high-sucrose diets.

Type
Papers of direct relevance to Clinical and Human Nutrition
Copyright
Copyright © The Nutrition Society 1985

References

REFERENCES

Eastwood, M. A. & Hamilton, D. (1968). Biochimica et Biophysira Acta 152, 165173.CrossRefGoogle Scholar
Freedland, R. A. (1967). Journal of Nutrition 91, 489495.CrossRefGoogle Scholar
Jefferys, D. B. (1974). Proceedings of the Nutrition Society 33, 11A12A.Google Scholar
Jenkins, D. J. A. (1979). Lancet ii, 12871290.CrossRefGoogle Scholar
Krebs, H. A. & Eggleston, L. V. (1974). Advances in Enzyme Regulation 12, 421434.CrossRefGoogle Scholar
Löwenstein, J. M. (1971). Journal of Biological Chemistry 246, 629632.CrossRefGoogle Scholar
Morgan, B., Heald, M., Atkin, S. D., Green, J. & Chain, E. B. (1974). British Journal of Nutrition 32, 447455.CrossRefGoogle Scholar
Myant, N. B. & Mitropoulos, K. A. (1977). Journal of Lipid Research 18, 135153.CrossRefGoogle Scholar
Rongstad, R. & Katz, J. (1979). Journal of Biological Chemistry 254, 1196911972.Google Scholar
Salmon, D. M. W., Bowen, N. L. & Hems, D. A. (1974). Biochemical Journal 142, 611618.CrossRefGoogle Scholar
Stanley, J. C. & Newsholme, E. A. (1985). British Journal of Nutrition 53, 215222.CrossRefGoogle Scholar
Trowell, H. C., Southgate, D. A. T., Wolever, T. M. S., Leeds, A. R., Gassull, M. A. & Jenkins, D. J. A. (1976). Lancet i, 967.CrossRefGoogle Scholar
Walters, R. L., McLean Baird, I., Davies, P. S., Hill, M. J., Drasar, B. S., Southgate, D. A. T., Green, J. & Morgan, B. (1975). British Medical Journal ii, 536538.CrossRefGoogle Scholar