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Protein-calorie malnutrition: Effect of deficient diets on enzyme levels of jejunal mucosa of rats

Published online by Cambridge University Press:  09 March 2007

E. Ann Burgess
Affiliation:
Queen Elizabeth Hospital for Children, Hackney Road, London, E 2
B. Levin
Affiliation:
Queen Elizabeth Hospital for Children, Hackney Road, London, E 2
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Abstract

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1. The effects of low-protein and protein-free diets on the levels of disaccharidase, peptidase and aldolase activities in the jejunal mucosa of rats were studied.

2. Maltase, palatinase and sucrase activities increased significantly after both types of feeding, although there was an initial fall with the protein-free diet.

3. The rise in lactase levels was, however, not so marked.

4. Glycyl-glycine and glycyl-leucine dipeptidase levels fell consistently with both diets.

5. Aldolase activities were generally unaltered, but tended to fall if the period of low-protein feeding was prolonged.

6. Enzyme levels rapidly returned to normal when the rats were given a normal diet after a period on a protein-deficient one.

7. It is suggested that the rise in disaccharidase and fall in peptidase levels are adaptive changes to the high-carbohydrate, low-protein diet, with diminished enzyme synthesis, due to lack of nitrogen, contributing to the lowered peptidase activities. The relevance of these results to disaccharide intolerance in chronic malnutrition, kwashiorkor and gastro-intestinal infection is discussed.

Type
Research Article
Copyright
Copyright © The Nutrition Society 1967

References

Alvarez, A. & Sas, J. (1961). Nature, Lond. 190, 826.CrossRefGoogle Scholar
Bowie, M. D., Brinkman, G. L. & Hansen, J. D. L. (1963). Lancet ii, 550.CrossRefGoogle Scholar
Burgess, E. A., Levin, B., Mahalanabis, D. & Tonge, R. E. (1964). Archs Dis. Childh. 39, 431.CrossRefGoogle Scholar
Cevini, G., Giovannini, M. & Careddu, P. (1962). Minerva paediat. 14, 831.Google Scholar
Dean, R. F. A. (1952). Br. med. J. ii, 791.CrossRefGoogle Scholar
Done, J. & Payne, P. R. (1959). Wld Rev. Nutr. Diet. 1, 227.Google Scholar
Heard, C. R. C. (1957). Proc. Nutr. Soc. 16, xl.Google Scholar
Josefsson, L. (1964). Nature, Lond. 204, 783.CrossRefGoogle Scholar
Josefsson, L. & Lindberg, T. (1965 a). Biochim. biophys. Acta 105, 149.CrossRefGoogle Scholar
Josefsson, L. & Lindberg, T. (1965 b). Biochim. biophys. Acta 105, 162.CrossRefGoogle Scholar
Levin, B., Oberholzer, V. G. & Whitehead, T. P. (1950). Analyst 75, 561.CrossRefGoogle Scholar
Leblond, C. P. & Stevens, C. E. (1948). Anat. Rec. 100, 357.CrossRefGoogle Scholar
Miller, D. S. & Payne, P. R. (1961). J. Nutr. 74, 413.CrossRefGoogle Scholar
Moore, S. & Stein, W. H. (1948). J. biol. Chem. 176, 367.CrossRefGoogle Scholar
Platt, B. S., Heard, C. R. C. & Stewart, J. C. (1964). In The Role of the Gastrointestinal Tract in Protein Metabolism. A Symposium Organized by the Council for International Organizations of Medical Sciences Established under the Joint Auspices of UNESCO and WHO, p. 227. [Munro, H. N., editor.] Oxford: Blackwell Scientific Publications.Google Scholar
Stanfield, J. P., Hutt, M. S. R. & Tunnicliffe, R. (1965). Lancet ii, 519.CrossRefGoogle Scholar
Sunshine, P. & Kretchmer, N. (1964). Pediatrics, Springfield, 34, 38.CrossRefGoogle Scholar