1 Division of Gastroenterology, Department of Pediatrics, Sainte Justine Hospital, and the University of Montreal, Montreal, Quebec, Canada
Enterokinase (enteropeptidase, E.C. 3,4,4,8) converts trypsinogen into active trypsin and is a key enzyme in the digestion of dietary proteins. Its absence results in gross protein malabsorption.1
In the present study, jejunal biopsy specimens were obtained from children with cystic fibrosis (CF), celiac disease (CD), or congenital exocrine pancreatic hypoplasia (CEPH) and from control subjects. Sections were examined histologically and homogenates were used for measurement of enterokinase and sucrase activities.
This work was undertaken because enterokinase is considered a brush border enzyme,2,3 the release of which into the intestinal lumen is influenced by pancreatic enzymes,4,5 and also because we have recently shown a small bowel mucosal dysfunction in patients with CF.6