Immunofluorescent localisation of enterokinase in human small intestine

SUMMARY The distribution of enterokinase in human intestine was studied in operative mucosal biopsies using specific antiserum to human enterokinase, previously purified to apparent homogeneity by affinity chromatography and immunoabsorption. Fluorescence was observed in the brush-border and glycocalyx of the duodenum and proximal 15 cm of jejunum distal to the D/J flexure. Distal jejunum and ileum as well as stomach and colon were consistently negative. Brunner's glands and goblet cells were never stained by specific antibody. Preliminary evidence was obtained that the human enterokinase molecule contains a specific antigenic determinant in its polypeptide component and a second determinant in the oligosaccharide moiety which cross-reacts with blood group A. Preliminary evidence was also obtained that mucosal synthesis of enterokinase may be impaired in jaundice due to carcinoma of the pancreas and induced in the small intestine distal to the normal limit of synthesis after pancreatico-duodenectomy. Enterokinase is the glycoprotein enzyme in the small intestine that triggers the activation of the zymogens in pancreatic juice by converting trypsinogen to trypsin; trypsin then activates the other zymogens o