Hostname: page-component-78c5997874-dh8gc Total loading time: 0 Render date: 2024-11-05T03:25:51.009Z Has data issue: false hasContentIssue false

[14C]leucine incorporation into proteins of pancreatic juice in rats fed soya-bean flour*

Published online by Cambridge University Press:  10 January 2017

U. R. Fölsch
Affiliation:
Department of Therapeutics, University of Dundee, Ninewells Hospital, Dundee DD2 1UB
K. G. Wormsley
Affiliation:
Department of Therapeutics, University of Dundee, Ninewells Hospital, Dundee DD2 1UB
Rights & Permissions [Opens in a new window]

Extract

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 effect of a diet containing a trypsin inhibitor on the incorporation of radioactively labelled leucine into the pancreatic proteins secreted during stimulation with cholecystokinin-pancreozymin (CCK) was studied in rats.

2. The total output of protein was significantly greater in the rats given raw soya-bean flour (RSF) compared with those given heat-inactivated soya-bean flour (HSF) (controls) in response to the sub- and supramaximal stimulation with CCK, but similar responses were obtained to maximal stimulation with CCK. Total protein output decreased continuously with time after reaching peak values at 90–120 min after the start of stimulation with CCK.

3. The total output of radioactively labelled protein in RSF-fed rats was not different from that of the controls with sub- and supramaximal dose rats of CCK, but was significantly lower than that of the controls in response to the dose rate of CCK which produced maximal rates of pancreatic secretion.

4. The specific activity of radioactively labelled protein increased continuously, while the output attained a constant rate during stimulation with all doses of CCK.

5. We concluded that feeding the trypsin inhibitor-containing diet led to increased secretion of stored pancreatic protein, while secretion of newly synthesized protein was not altered. During the course of prolonged stimulation with CCK, irrespective of diet, there was increasing secretion of the newly synthesized protein compared with the pre-existing stored proteins of the pancreas, but it was unable to compensate for the decreased secretion of pre-formed protein.

Type
Papers of direct relevance to Clinical and Human Nutrition
Copyright
Copyright © The Authors 1976

Footnotes

*

Presented at the 7th Symposium of the European Pancreatic Club, 1974.

References

Bernhardt, F. W. & Tomarelli, R. (1966). J. Nutr. 89, 495.CrossRefGoogle Scholar
Creutzfeldt, W., Arnold, C., Creutzfeldt, C., Deuticke, U., Frerichs, H. & Track, N. S. (1973). Diabetologia 9, 217.CrossRefGoogle Scholar
Fölsch, U. R., Winkler, K. & Wormsley, K. G. (1974 a). In Aktionen und Interaktionen, p. 360 [Becker, V., editor]. Baden-Baden: G. Witzstrock.Google Scholar
Fölsch, U. R., Winkler, K. & Wormsley, K. G. (1974 b). Digestion 11, 161.CrossRefGoogle Scholar
Fölsch, U. R. & Wormsley, K. G. (1973). J. Physiol., Land. 245, 79.CrossRefGoogle Scholar
Fölsch, U. R. & Wormsley, K. G. (1974). Scand. J. Gastroent. 9, 679.CrossRefGoogle Scholar
Gan, J. C. & Jeffay, H. (1967). Biochim. biophys. Acta 148, 448.CrossRefGoogle Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). J. biol. Chem. 193, 265.CrossRefGoogle Scholar
Porter, G. (1963). In Animals for Research, [Lane-Petter, W., editor]. New York: Academic Press.Google Scholar
Rothman, S. S. (1970). Am.J. Physiol. 219, 1652.CrossRefGoogle Scholar
Rothman, S. S. (1975). Am.J. Physiol. 228, 1828.CrossRefGoogle Scholar
Rothman, S. S. & Isenman, L. D. (1974). Am.J. Physiol. 226, 1082.CrossRefGoogle Scholar
Schramm, M., Sharoni, Y. & Eimerl, S. (1976). Biologie Gastro-ent. (In the Press.)Google Scholar
Track, N. S., Frerichs, H. & Creutzfeldt, W. (1974). Horm. Metab. Res. Suppl. 5, 97.Google Scholar
Warner, R. G. (1962). Nutrient Requirements of the Laboratory Rat. National Research Council Committee on Animal Nutrition Publication no. 990 Washington, DC: National Academy of Sciences – National Research Council.Google Scholar