Catalytically active enterokinase in human bile.
Enterokinase activates trypsinogen very rapidly and is itself resistant to proteolysis and endogenous inhibitors in blood and pancreas. Using a novel one-stage specific catalytic assay capable of detecting enterokinase in the presence of trypsin inhibitors, we have positively identified catalytically active enterokinase in human bile in each of 14 patients studied. Since the presence of active enterokinase in human bile was not explicable by duodeno-biliary reflux, enterokinase must have followed the pathway from gut to blood to liver to bile, previously identified in greater detail experimentally. We suggest that entry into the pancreatic duct system of bile-borne active enterokinase from the common bile duct may trigger necrotising acute pancreatitis.
D000208:Acute Disease; D000328:Adult; D000368:Aged; D001646:Bile / Q000201:enzymology*; D002850:Chromatography, Gel; D010450:Endopeptidases / Q000378:metabolism*; D004765:Enteropeptidase / Q000378:metabolism*; D005260:Female; D006801:Humans; D008297:Male; D008722:Methods; D008875:Middle Aged; D008970:Molecular Weight; D010195:Pancreatitis / Q000201:enzymology; D013997:Time Factors; D014362:Trypsinogen / Q000378:metabolism
D014362:Trypsinogen; D010450:Endopeptidases; D004765:Enteropeptidase