Abstract
Acute pancreatitis was induced in dogs by injecting into the pancreatic duct a mixture of taurocholate and trypsin. Exudate from pancreas was collected outside the body by a special technique in separate portions each covering one hour.
All exudates were found to possess ability to break down lecithin by phospholipase and lysophospholipase action. Calcium, bile, and taurocholate stimulated and EDTA inhibited the degradation of lecithin. The phospholipase activity was studied in the hourly collected portions of pancreatic exudate. It was very high and had a maximum in the portion collected during the first hour, being lower and levelling out in the portions collected during the 4 to 7 hour periods. Amylase activity paralleled the phospholipase activity of the exudate.
The demonstration of an early release in acute pancreatitis of lecithin-hydrolyzing enzyme systems in pancreatic exudate may have bearings on the pathogenesis of acute pancreatitis.
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