alpha-chymotrypsin and Giardiasis

We studied six patients with giardiasis (five males, one female), median age 3.5 yr (range 1-11) and 12 healthy control subjects (10 males, 2 females), median age 3.5 yr (range 1-10). Intestinal biopsy and a contemporaneous secretin-cerulein test were performed in all patients, and fecal chymotrypsin was also assayed. Intestinal biopsy was normal in five of the six patients with giardiasis, whereas one of the six presented a partial atrophy of the intestinal villi. The secretin-cerulein test (1 CU/kg of secretin + 75 ng/kg of cerulein) did not show any significant difference between values in the outputs of chymotrypsin, lipase, phospholipase, and bicarbonate obtained in patients and in controls; however, in the one patient with partial intestinal mucosal atrophy, all enzymatic activity levels were below the normal limit for our laboratory. Furthermore, the mean values of fecal chymotrypsin concentration did not differ between the two groups. Fecal chymotrypsin was also reduced in the patient with an abnormal secretin-cerulein test; a second assay performed 3 mo after the suspension of treatment (Metronidazole), however, showed a normal chymotrypsin concentration.

Topics: Ceruletide; Child; Child, Preschool; Chymotrypsin; Feces; Female; Giardiasis; Humans; Infant; Male; Pancreas; Pancreatic Juice; Secretin

Agarose gel electrophoresis (at pH 8.6) was used for qualitative determination of pancreatic enzymes in duodenal juice. The various enzymes were identified by staining techniques with specific chromogenic substrates, by quantitative determination of enzymes in eluates of gel slices, and by immunoelectrophoresis. The various protein bands corresponded to the following enzymes (from the anode to the cathode): chymotrypsin, trypsin, carboxypeptidase A, chymotrypsin, amylase (around the slit), lipase, elastase, and trypsin. The method was applied to a study of exocrine pancreatic function in 10 adults and 83 children suspected of having malabsorption. The duodenal juice, also analyzed for trypsin and amylase content, was collected in fasting condition and after a test meal of water. In patients with normal pancreatic function, all the enzyme bands were present and easy to recognize. In 87 patients carboxypeptidase A was present as two bands in 68 (80%), anodal trypsin as two bands in 39 (45%), and cathodal trypsin as two bands in 85 (97%). Electrophoresis of duodenal juice gave as much information from the fasting sample as after the test meal. Six children with pancreatic insufficiency (cystic fibrosis and Shwachmar's syndrome) had no or only faintly stained enzyme bands and a strongly stained albumin-containing band most anodally. The method is simple, rapid, and useful in routine work. The combination of this qualitative test with a quantitative one (e.g. trypsin determination) provides good information about exocrine pancreatic function.

Topics: Adolescent; Adult; Amylases; Carboxypeptidases; Celiac Disease; Child; Child, Preschool; Chymotrypsin; Duodenum; Electrophoresis; Electrophoresis, Agar Gel; Female; Food Hypersensitivity; Giardiasis; Humans; Immunoelectrophoresis; Infant; Malabsorption Syndromes; Male; Pancreatic Diseases; Pancreatic Elastase; Pancreatic Juice; Trypsin