Hostname: page-component-7bb8b95d7b-wpx69 Total loading time: 0 Render date: 2024-09-12T00:40:40.119Z Has data issue: false hasContentIssue false

The activities of some metabolic enzymes in the intestines of germ-free and conventional chicks

Published online by Cambridge University Press:  24 July 2007

Maureen F. Palmer
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading, Berkshire RG2 9AT
B. A. Rolls
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading, Berkshire RG2 9AT
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 metabolic enzymes alkaline phosphatase (EC 3. 1. 3. 1), acid phosphatase (EC 3. 1. 3. 2) and isocitrate dehydrogenase (EC 1. 1. 1. 42) were measured in mucosal homogenates and these enzymes, together with glucose-6-phosphatase (EC 3. 1. 3. 9), were measured in homogenates of isolated enterocytes from germ-free (GF) and conventional (CV) chicks which were either fed continuously until they were killed or were subjected to a 16 h fast before killing.

2. The intestine of the GF chicks was generally lighter than that of the CV controls. The activity of alkaline phosphatase was greater in the mucosal homogenates of the CV chicks compared with the GF birds, but the concentrations of acid phosphatase and isocitric dehydrogenase were not different in the two groups. In the isolated enterocytes the concentration of all enzymes expressed per mg DNA, except alkaline phosphatase, was higher in the GF chicks. Expressed per mg protein there was no significant difference in enzyme activity in the two groups.

3. Fasting caused a reduction in intestinal weight and total mucosal protein in both groups but the reduction was greater in the GF chicks compared with the CV controls. In the GF chicks, fasting caused a significant fall in acid phosphatase and isocitric dehydrogenase activities of the mucosal homogenate, whereas in the CV chicks only acid phosphatase fell to a significant extent. In the isolated enterocytes feeding caused a marked fall in protein per mg DNA in the CV chicks; fasting tended to reduce enzyme concentrations in the GF chicks but to have less effect in the CV group except for alkaline phosphatase where there was a marked rise in activity.

4. It is suggested that the difference in enzyme activities in the mucosal homogenates and isolated enterocytes might result from (a) the presence of a much greater lamina propria in the CV compared with the GF chicks and (b) the greater mitotic activity in the fed CV chicks yielding a much larger number of smaller immature cells.

Type
Research Article
Copyright
Copyright © The Nutrition Society 1983

References

Allen, R. J. L. (1940). Biochemical Journal 34, 858865.CrossRefGoogle Scholar
Brandenberger, H. & Hanson, R. (1953). Helvetica Chimica Acta 36, 900906.Google Scholar
Burton, K. (1956). Biochemical Journal 62, 315323.CrossRefGoogle Scholar
Coates, M. E. & Fuller, R. (1977). In Microbial Ecology of the Gut, pp. 312342. [Edwards, R. T. J. and Bauchop, T. editors]. London and New York: Academic Press.Google Scholar
Coates, M. E., Fuller, R., Harrison, G. F.Lev, M. & Suffolk, S. F. (1963). British Journal of Nutrition 17, 141150.CrossRefGoogle Scholar
Fiske, C. H. & SubbaRow, Y. (1925). Journal of Biological Chemistry 66, 375400.Google Scholar
Fleck, A. & Munro, H. N. (1962). Biochimica et Biophysica Acta 55, 571583.CrossRefGoogle Scholar
Fuller, R. (1968). In The Germ-free Animal in Research, pp. 3745 [Coates, M. E. editor]. London and New York: Academic Press.Google Scholar
Garland, P. B. (1968). In The Metabolic Roles of Citrate, pp. 4160 [Goodwin, T. W. editor]. London: Academic Press.Google Scholar
Gordon, H. A. & Bruckner-Kardoss, E. (1958). Antibiotics Annual 10121019.Google Scholar
Gordon, H. A. & Bruckner-Kardoss, E. (1961). Acta Anatomica 44, 210225.CrossRefGoogle Scholar
Harrison, G. G. (1969). Laboratory Animals 3, 5159.CrossRefGoogle Scholar
Inglis, N. J., Krant, M. J. & Fishman, W. H. (1967). Proceedings of the Society for Experimental Biology and Medicine 124, 699702.CrossRefGoogle Scholar
Kimmich, G. A. (1970). Biochemistry, Easton 9, 36593677.CrossRefGoogle Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). Journal of Biological Chemistry 193, 265275.CrossRefGoogle Scholar
Lygre, D. G. & Nordlie, R. C. (1968). Biochemistry, Easton, 7, 32193226.CrossRefGoogle Scholar
Miller, D. & Crane, R. K. (1961). Biochimica et Biophysica Acta 52, 293298.CrossRefGoogle Scholar
Ochoa, S. (1948). Journal of Biological Chemistry 174, 133157.CrossRefGoogle Scholar
Rolls, B. A., Turvey, A. & Coates, M. E. (1978). British Journal of Nutrition 39, 9198.CrossRefGoogle Scholar
Siddons, R. C. & Coates, M. E. (1971). British Journal of Nutrition 27, 101112.CrossRefGoogle Scholar
Smith, C. M. & Plaut, G. W. E. (1979). European Journal of Biochemistry 97, 283295.CrossRefGoogle Scholar
Swanson, M. A. (1955). In Methods in Enzymology, vol. 2, pp. 541543 [Colwich, S. P. and Kaplan, N. O. editors]. London and New York: Academic Press.Google Scholar
Whitt, D. D. & Savage, D. C. (1980). Infection and Immunity 29, 144151.Google Scholar