Layer_1986_Am.J.Physiol_251_G475

To determine survival of pancreatic enzymes during small intestinal aboral transit in humans, seven healthy volunteers were intubated with an oroileal tube. By using nonabsorbable markers we measured the cumulative amount of lipase, trypsin, and amylase activities and lipase and trypsin immunoreactivities delivered postprandially to the duodenum, midjejunum, and terminal ileum. We found that as the enzymes moved from duodenum to ileum, 74% of amylase activity, 22% of trypsin activity, and 1% of lipase activity survived transit. Enzymatic activity and immunoreactivity of trypsin and lipase disappeared at different rates, suggesting that for these enzymes the sites of enzymatic activity and immunorecognition are not identical. Since tryptic activity is present even in the absence of immunorecognizable trypsin, complete structural integrity of the trypsin molecule may not be essential for its enzymatic activity. The short intraluminal survival of lipolytic activity may partially explain why patients with progressive exocrine pancreatic insufficiency malabsorb fat earlier than other nutrients.