Amylase in Pancreas, Intestine, Liver, and Serum During Fasting, Non-protein Diet and Realimentation.
- 1 April 1959
- journal article
- research article
- Published by Frontiers Media SA in Experimental Biology and Medicine
- Vol. 100 (4) , 834-837
- https://doi.org/10.3181/00379727-100-24795
Abstract
Male rats were fasted for 8 days or fed non-protein diet for 16 days. Amylase activity was determined at intervals in pancreas, small gut, liver and serum. In each instance fasting caused sharp and parallel drops in amylase activity. Feeding non-protein diet 2-4 days seemed to spare amylase in small gut and serum. Liver fluctuated in the first 4 days and then remained at half normal activity for 16 days. Pancreatic amylase activity was depleted more on non-protein diet than in fasting. Feeding induces increased secretion of pancreatic amylase which, with other endogenous proteins, is probably hydrolyzed in the intestinal lumen and its amino acids absorbed. The data suggest that intestinal mucosa by virtue of its absorptive function is able to remove amino acids for protein synthesis directly from gut contents, and that the liver has next choice through the portal system. Finally the pancreas and other tissues are supplied by way of the peripheral circulation.Keywords
This publication has 2 references indexed in Scilit:
- The Digestion of Proteins in VivoJournal of Nutrition, 1955
- A PHOTOMETRIC METHOD FOR THE DETERMINATION OF α-AMYLASE IN BLOOD AND URINE, WITH USE OF THE STARCH-IODINE COLORJournal of Biological Chemistry, 1949