Hostname: page-component-cd9895bd7-hc48f Total loading time: 0 Render date: 2024-12-22T21:51:17.901Z Has data issue: false hasContentIssue false
  • English
  • Français

The use of a semi-synthetic liquid diet for the supply of ethanol to rats and its effect on lysosomal enzyme activities in the liver*

Published online by Cambridge University Press:  24 July 2007

L. Pilström ,
E. Fellenius  and
K.-H. Kiessling
L. Pilström
Affiliation:
Alcohol Research Group, Swedish Medical Research Council, Institute of Zoophysiology, University of Uppsala, Uppsala, Sweden
E. Fellenius
Affiliation:
Alcohol Research Group, Swedish Medical Research Council, Institute of Zoophysiology, University of Uppsala, Uppsala, Sweden
K.-H. Kiessling
Affiliation:
Alcohol Research Group, Swedish Medical Research Council, Institute of Zoophysiology, University of Uppsala, Uppsala, Sweden
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. A liquid diet is described for the supply of ethanol to rats with a constant proportion of energy equivalents from different sources. In this diet, a protein-enriched, dry, milk powder is used as the protein source.

2. The diet was used in a two-group experiment lasting for 80 d in which the rats were fed ad lib. The consumption was 120 ml/d per rat in the control group, whereas in the ethanol-consuming group the consumpton was only 40 ml/d per rat at the start of the experiment and rose to and remained at 80 ml/d per rat after 20 d.

3. The control group grew normally. In the ethanol-consuming group, there was an initial loss of body-weight; after 20 d there was some increase in body-weight but growth was slower than in the control group. The smaller food intake in the ethanol group was not wholly caused by the lower body-weight.

4. The free and total activities of acid phosphatase (EC 3·1·3·2) and β-glucuronidase (EC 3·2·1·31) were estimated in the liver after 10, 20, 30, 40, 60 and 80 d. Neither the free nor the total activity of acid phosphatase changed significantly during the experiment. The ratio of free activity to total activity increased significantly after 20–40 d of treatment with ethanol. The free and total activities of β-glucuronidase were significantly increased after 10 d of treatment with ethanol, but this difference could not be shown after prolonged treatment.

Type
General Nutrition
Information
British Journal of Nutrition , Volume 29 , Issue 2 , March 1973 , pp. 297 - 306
Copyright
Copyright © The Nutrition Society 1973

References

REFERENCES

Bramhall, S., Noack, N., Wu, M. & Loewenberg, J. R. (1969). Analyt. Biochem. 31, 146.Google Scholar
Dajani, R. M., Ghandur-Mnaymneh, L., Harrison, M. & Nassar, T. (1965). J. Nutr. 86, 29.CrossRefGoogle Scholar
DeCarli, L. M. & Lieber, C. S. (1966). Fedn Proc. Fedn Am. Socs exp. Biol. 25, 304.Google Scholar
DeCarli, L. M. & Lieber, C. S. (1967). J. Nutr. 91, 331.CrossRefGoogle Scholar
Filkins, J. P. (1970). Am. J. Physiol. 219, 923.CrossRefGoogle Scholar
Flax, M. H. & Tisdale, W. A. (1964). Am. J. Path. 44, 441.Google Scholar
French, S. W. (1968). Gastroenterology 54, 1106.CrossRefGoogle Scholar
French, S. W. & Morin, R. J. (1969). In Biochemical and Clinical Aspects of Alcohol Metabolism p. 123 [Sardesai, V. M., editor]. Springfield, Ill: C. C. Thomas.Google Scholar
Germer, W. D. & Choi, H. (1959). Z. Ges. exp. Med. 131, 238.CrossRefGoogle Scholar
Gros, H. (1971). In Alcohol and the Liver, International Symposium, 2-4 Oct. 1970, Freiburg p. 353 [Gerok, W., Sickinger, K. and Hennekeuser, H. H., editors]. Stuttgart: F. K. Schattauer Verlag.Google Scholar
Hartman, A. D. & Di Luzio, N. R. (1968). Proc. Soc. exp. Biol. Med. 127, 270.Google Scholar
Jabbari, M., Baker, H. & Leevy, C. M. (1965). Am.J. clin. Nutr. 16, 382.Google Scholar
Jones, D. P. & Greene, E. A. (1966). Am. J. clin. Nutr. 18, 350.Google Scholar
Kiessling, K.-H. & Pilström, L. (1966 a). Q. Jl Stud. Alcohol 27, 189.Google Scholar
Kiessling, K.-H. & Pilström, L. (1966 b). Acta pharmac. tox. 24, 103.Google Scholar
Klatskin, G., Gewin, H. M. & Krehl, W. A. (1951). Yale J. Biol. Med. 23, 317.Google Scholar
Lieber, C. S. & DeCarli, L. M. (1970). Am. J. clin. Nutr. 23, 474.CrossRefGoogle Scholar
Lieber, C. S., Jones, D. P., Mendelson, J. & DeCarli, L. M. (1963). Trans. Ass. Am. Physns 76, 289.Google Scholar
Oudea, M. C., Launay, A. N., Quénéhervé, S. & Oudea, P. (1970). Rev. eur. Étud. clin. biol. 15, 748.Google Scholar
Porta, E. A., Hartroft, W. S. & de la Iglesia, F. A. (1965). Lab. Invest. 14, 1437.Google Scholar
Porta, E. A., Koch, O. R. & Hartroft, W. S. (1969). Fedn Proc. Fedn Am. Socs exp. Biol. 28, 626.Google Scholar
Saville, P. D. & Lieber, C. S. (1965). J. Nutr. 87, 477.CrossRefGoogle Scholar
Slater, T. F. (1969). In Lysosomes in Biology and Pathology Vol. 1, p. 467 [DingIe, J. T. and Fell, B., editors]. Amsterdam: North-Holland Publ. Co.Google Scholar
Wallgren, H., Ahlqvist, J., Åhman, K. & Suomalainen, H. (1967). Br. J. Nutr. 21, 643.CrossRefGoogle Scholar
Weissman, G. (1969). In Lysosomes in Biology and Pathology Vol. 1, p. 276 [Dingle, J. T. and Fell, B., editors]. Amsterdam: North-Holland Publ. Co.Google Scholar
Zakim, D. & Green, J. (1968). Proc. Soc. exp, Biol. Med. 127, 138.Google Scholar
Zucker, L. & Zucker, T. F. (1941–1942). J. gen. Physiol. 25, 445.CrossRefGoogle Scholar