Pancreatic Elastase is an anionic endoprotease of the serine protease family. Together with other digestive enzymes it is synthesized as an inactive pro-enzyme in the acinar cells of the pancreas and is secreted into the duodenum.
After activation, pancreatic elastase cleaves peptides after neutral amino acids. Pancreatic elastase is mainly bound to bile salts during intestinal transit and is not degraded. In human faeces it is 5 - 6 times more concentrated than in pancreatic juice making it a viable analyte to measure.
The concentration of pancreatic elastase in stool reflects the secretory capacity of the pancreas and so can be a useful tool in determining or excluding exocrine pancreatic insufficiency.