Mar 1, 1979

Lysosomal enzymes in pure pancreatic juice from normal healthy volunteers and chronic alcoholics

Digestive Diseases and Sciences
H RinderknechtH H Koyama

Abstract

Investigation of pure human pancreatic juice obtained by direct cannulation of the main pancreatic duct of 11 healthy volunteer subjects and 10 chronic alcoholics without detectable pancreatic disease revealed the presence of numerous acid hydrolases in this secretion. The pH optimal and substrate specificities of these enzymes suggest that they are of lysosomal origin. Stimulation of the pancreas by injection of cholecystokinin-pancreozymin (CCK-PZ) (1 Ivy dog unit/kg) resulted in a striking increase in activity of some of these hydrolases (N-acetyl-beta-D-glucosaminidase, arylsulfatase, etc.) similar to that observed for trypsin, amylase, and other pancreatic digestive enzymes. In a second group of hydrolases (beta-D-glucuronidase, leucine naphthylamidase, etc.) the effect of this hormone was greatly reduced or absent, particularly in normal individuals. In chronic alcoholics enzyme activity in response to CCK-PZ injection was greater than in normal subjects. Although this increase achieved statistical significance (P less than 0.05) in the case of beta-D-glucuronidase only, it was observed for all lysosomal hydrolases tested and suggests either increased synthesis or a more facile release of these enzymes from the pancreas o...Continue Reading

  • References9
  • Citations31

References

  • References9
  • Citations31

Citations

Mentioned in this Paper

Beta-N-Acetylglucosaminidase
Cholecystokinin
CCK-33
Enzymes, antithrombotic
Benign Tumor of Pancreas
Beta-glucuronidase
Aminopeptidase
Alcohol Abuse
Process of Secretion
Secrepan

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