Elastase Activity in Human Pancreatic Secretions

Abstract

IN 1949, Balo and Banga¹ first reported the isolation of the pancreatic enzyme elastase, which was unique in its ability to render soluble elastin (an important structural component of arteries, veins, skin and lung). This enzyme was first believed to be mucolytic in action, but it is now established that it is also a potent proteolytic agent². Kokas, Foldes and Banga³, in a series of acute experiments, cannulated the main pancreatic duct of dogs and reported demonstrable elastolytic activity in canine pancreatic secretions. Grant and Robbins⁴ in a similar experiment reported that elastase in the pancreas is inactive. They hypothesize that the inactive ‘proelastase’ must be activated (by small amounts of crystalline trypsin or enterokinase) before elastolytic activity can be demonstrated.