|
|
||||||||
AJP - Gastrointestinal and Liver Physiology, Vol 254, Issue 5 775-G780, Copyright © 1988 by American Physiological Society
ARTICLES |
J. L. Rosenblum, C. L. Irwin and D. H. Alpers
Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, St. Louis, Missouri.
Salivary-type amylase may significantly contribute to duodenal starch hydrolysis in exocrine pancreatic insufficiency, provided that gastric inactivation does not occur. We investigated the effect of starch and its hydrolytic products, therefore, on salivary amylase activity in vitro at low pH. When incubated at pH 3 in the presence of 1% starch, 56% of the initial activity of amylase purified from saliva remained after 60 min at 37 degrees C compared with only 6% without starch. Similar protection of amylolytic activity was observed using human milk, which also contains a salivary-type amylase. In addition, partially hydrolyzed starch protected salivary amylase activity at pH 3, and purified glucose oligomers ranging in length from two to seven glucose molecules protected amylase in a concentration-dependent manner. Lactose, sucrose, and glucose, however, were ineffective in sparing amylase. Starch protected amylase activity even in the presence of pepsin, and maltotriose conferred striking protection below pH 3. These studies indicate that salivary-type isoamylases are protected in a simulated gastric environment by substrates of amylase as well as its end products of hydrolysis.
This article has been cited by other articles:
![]() |
F. K. Hamra, S. L. Eber, D. T. Chin, M. G. Currie, and L. R. Forte Regulation of intestinal uroguanylin/guanylin receptor-mediated responses by mucosal acidity PNAS, March 18, 1997; 94(6): 2705 - 2710. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| Visit Other APS Journals Online |