Hostname: page-component-5c6d5d7d68-7tdvq Total loading time: 0 Render date: 2024-08-19T02:56:27.409Z Has data issue: false hasContentIssue false

Artificial rearing of pigs

2.* The time course of milk protein digestion and proteolytic enzyme secretion in the 28-day-old pig

Published online by Cambridge University Press:  09 March 2007

R. Braude
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading RG2 9 A T
M.J. Newport
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading RG2 9 A T
J.W. Porter
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading RG2 9 A T
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 time course of digestion of milk protein was studied in the 28-d-old pig given a test meal of homogenized cow's milk after a preliminary starvation period.

2. The milk was found to clot in the stomach 15–30 min after the meal. The soluble or ‘whey’ fraction of the stomach contents rapidly passed into the small intestine. Most of the clotted digesta had also left the stomach z h after the meal.

3. The distribution of digesta was studied in six equal segments of the small intestine. In general, there were no significant increases in the amount of intestinal contents at any time after the meal when compared with those in starved pigs, suggesting that digestion of milk at this age is a very efficient process.

4. Fractionation of the soluble digesta from the stomach and small intestine in Sephadex G-25 indicated that relatively little proteolysis occurred in the stomach, but in the small intestine digestion proceeded rapidly, producing a considerable increase in free amino acids in the mid-region.

5. The level of proteolytic enzyme activity in the stomach wall was elevated at 15 min after the meal, but thereafter returned rapidly to the prefeeding levels. Increasing the level of feeding increased the enzyme activity of the digesta and stomach wall. The enzyme activity appeared to be mainly adsorbed by the stomach clot.

6. The proteolytic enzyme activity in the pancreas was unaffected by the meal. However, the activity in the contents of the small intestine increased after the meal, reaching a maximum value at 45 min. Some accumulation of enzymes was found in the lower part of the small intestine, except in the region of the distal ileum where a marked decline in enzyme activity occurred. Increasing the level of feeding increased the proteolytic enzyme activity in the contents of the small intestine.

7. The soluble marker polyethylene glycol was not entirely satisfactory as an indicator of the rate of passage of digesta. The concentration of the marker was found to be greater in the soluble stomach fraction than in the clot shortly after the milk had been ingested. The transit time of the marker from ingestion to the terminal ileum was 2–3 h.

Type
Research Article
Copyright
Copyright © The Nutrition Society 1970

References

REFERENCES

Ash, R. W. (1964). J. Physiol., Lond. 172, 425.Google Scholar
Braude, R., Glascock, R. F., Newport, M. J. & Porter, J. W. G. (1969). J. Dairy Res. 36, 129.CrossRefGoogle Scholar
Braude, R., Mitchell, K. G., Newport, M. J. & Porter, J. W. G. (1970). Br. J. Nutr. 24, 501.CrossRefGoogle Scholar
Chen, M. L., Rogers, Q. R. & Harper, A. E. (1962). J. Nutr. 76, 235.Google Scholar
Clark, A. J., Hays, V. W., McCall, J. T. & Speer, V. C. (1963). J. Anim. Sci. 22, 1118.CrossRefGoogle Scholar
Ford, J. E. (1965). Br. J. Nutr. 19, 277.CrossRefGoogle Scholar
Guminski, T. & Naismith, D. J. (1959). Proc. Nutr. Soc.18, xxxv.Google Scholar
Harper, A. E. (1965). Can. J. Biochem. 43, 1589.CrossRefGoogle Scholar
Henschel, M. J., Hill, W. B. & Porter, J. W. G. (1961).Proc. Nutr. Soc. 20, xl.Google Scholar
Kidder, D. E. & Manners, M. J. (1968). Proc. Nutr. Soc. 27, 46A.Google Scholar
Kidder, D. E., Manners, M. J. & McCrea, M. R. (1961). Res. vet. Sci. 2, 227.CrossRefGoogle Scholar
Kvasnitskii, A. V. (1951). Fiziologiya Pishchevareniya u Sviney p. 132. Moscow: Sel'khozgiz.Google Scholar
Kvasnitskii, A. V. & Bakeeva, E. N. (1940). Trud. Inst. Svinovod., Kiev. 15, 43.Google Scholar
Lepkovsky, S., Furuta, F., Ozone, K., Koike, T. & Wagner, M. (1966). Br. J. Nutr. 20, 257.CrossRefGoogle Scholar
Maner, J. H., Pond, W. G., Loosli, J. K. & Lowrey, R. S. (1962). J. Anim. Sci. 21, 49.CrossRefGoogle Scholar
Moore, S. & Stein, W. H. (1954). J. biol. Chem. 211, 907.Google Scholar
Mylrea, P. J. (1966). Res. vet. Sci. 7, 333.CrossRefGoogle Scholar
Naismith, D. J., Mittwoch, A. & Platt, B. S. (1969). Br. J. Nutr. 23, 683.Google Scholar
Noakes, D. E., Cranwell, P. D. & Hill, K. J. (1968). Proc. Nutr. Soc. 27, 2A.Google Scholar
Noakes, D. E., Hill, K. J., Freeman, C. P. & Annison, E. F. (1967). Proc. Nutr. Soc. 26, vi.Google Scholar
Padalikova, D. (1964). Cslká. Fysiol. 13, 255.Google Scholar
Pekas, J. C., Thompson, A. M. & Hays, V. W. (1966). J. Anim. Sci. 25, 113.CrossRefGoogle Scholar
Pelot, D. & Grossman, M. I. (1962). Am. J. Physiol. 202, 285.CrossRefGoogle Scholar
Peraino, C., Rogers, Q. R., Yoshida, M., Chen, M.-L. & Harper, A. E. (1959). Can. J. Biochem. Physiol. 37, 1475.Google Scholar
Platt, B. S. (1961). Fedn Proc. Fedn Am. Socs exp. Biol. 20, Suppl. 7, p. 188.Google Scholar
Rogers, Q. R. & Harper, A. E. (1964). In The Role of the Gastrointestinal Tract in Protein Metabolism p. 3 ]Munro, H. N., editor[. Oxford: Blackwell Scientific Publications.Google Scholar
Rowland, S. J. (1938). J. Dairy Res. 9, 42.CrossRefGoogle Scholar
Smith, R. H. (1958). Nature, Lond. 182, 260.Google Scholar
Smith, R. H. (1964). J. Physiol., Lond. 172, 305.CrossRefGoogle Scholar
Walker, D. M. (1959). J. agric. Sci., Camb. 52, 352.CrossRefGoogle Scholar
Washburn, R. M. & Jones, C. H. (1916).Bull. Vt agric. Exp. Stn no. 195.Google Scholar
Zebrowska, T. (1968). Br. J. Nutr. 22, 483.Google Scholar