alpha-chymotrypsin and Pancreatic-Diseases

Exocrine pancreatic insufficiency in children can lead to lifelong complications related to malnutrition and poor growth. The clinical presentation can be subtle in the early stages of insufficiency as the large functional capacity of the pancreas is gradually lost. The pediatrician plays a crucial role in the early identification of these children to ensure a timely referral so that a diagnosis can be made and therapy initiated. Early nutritional therapy allows for prevention and correction of deficiencies, which leads to improved outcomes and survival. When insufficiency is suspected, the workup should start with an indirect test of exocrine pancreatic function, such as fecal elastase, to establish the diagnosis. Once a diagnosis is established, further testing to delineate the etiology should be pursued, with cystic fibrosis being high on the differential list and assessed for with a sweat test. Assessment of anthropometry at every visit is key, as is monitoring of laboratory parameters and physical examination findings that are suggestive of malabsorption and malnutrition. The mainstay of management is administration of exogenous pancreatic enzymes to facilitate digestion and absorption. [Pediatr Ann. 2019;48(11):e441-e447.].

Topics: Acyl-CoA Dehydrogenase, Long-Chain; Anus, Imperforate; Child; Child Nutrition Disorders; Chymotrypsin; Congenital Bone Marrow Failure Syndromes; Cystic Fibrosis; Dietary Fats; Ectodermal Dysplasia; Enzyme Replacement Therapy; Exocrine Pancreatic Insufficiency; Feces; Growth Disorders; Hearing Loss, Sensorineural; Humans; Hypothyroidism; Intellectual Disability; Lipid Metabolism, Inborn Errors; Mitochondrial Diseases; Muscular Diseases; Nose; Nutrition Assessment; Pancreas; Pancreatic Diseases; Pancreatic Elastase; Pancreatic Function Tests; Pancreatitis, Chronic; Shwachman-Diamond Syndrome; Steatorrhea; Trypsinogen

Topics: Chymotrypsin; Humans; Pancreatic Diseases

Topics: Chymotrypsin; Feces; Humans; Pancreatic Diseases

Topics: 4-Aminobenzoic Acid; Amylases; Bicarbonates; Chymotrypsin; Feces; Fluoresceins; Humans; Isoamylase; Pancreatic Diseases; Pancreatic Function Tests; para-Aminobenzoates; Saliva; Trypsin

Topics: 4-Aminobenzoic Acid; Alkaline Phosphatase; Amylases; Animals; Atrophy; Carnivora; Chymotrypsin; Dog Diseases; Dogs; Exocrine Pancreatic Insufficiency; Feces; Lipase; Pancreas; Pancreatic Diseases; Pancreatic Neoplasms; Pancreatitis; Trypsin

The hitherto existing results of determinations of enzymatic activities in stool are presented in this review. The chymotrypsin activity is diminished in advanced exocrine pancreatic insufficiency. The faecal alpha-amylase activity has up to now no significance in the diagnosis of pancreatic diseases. Up to five amylolytic enzyme activities are detectable. The alkaline phosphatase is mostly of intestinal origin. Up to 4 enzyme bands can be exhibited with the disc electrophoresis in polyacrylamide gel. Lysozyme and N-Acetyl-beta-D-glycosaminidase can also be detected in stool.

Topics: Alkaline Phosphatase; Amylases; Animals; Chymotrypsin; Colitis, Ulcerative; Cystic Fibrosis; Enzyme Induction; Feces; Hepatitis, Viral, Human; Hexosaminidases; Humans; Intestinal Mucosa; Malabsorption Syndromes; Muramidase; Pancreatic Diseases; Protozoan Infections; Rats; Trypsin

Topics: 4-Aminobenzoic Acid; Amino Acids, Essential; Bicarbonates; Body Fluids; Cholecystokinin; Chymotrypsin; Duodenum; Feces; Humans; Meat; Pancreas; Pancreatic Diseases; para-Aminobenzoates; Perfusion; Radiography; Radioisotopes; Secretin; Staining and Labeling; Trypsin; Tyrosine

Topics: Amylases; Bicarbonates; Biliary Tract Diseases; Carbohydrate Metabolism; Child; Cholecystokinin; Chymotrypsin; Duodenum; Feces; Humans; Lipase; Methods; Pancreas; Pancreatic Diseases; Pancreatic Hormones; Pancreatic Neoplasms; Pancreatitis; Radiography; Secretin; Trypsin

Topics: Adolescent; Adult; Aminobenzoates; Amylases; Animals; Bicarbonates; Catalase; Cholecystokinin; Chymotrypsin; Clinical Enzyme Tests; Female; Haplorhini; Humans; Intestinal Mucosa; Lipase; Lipid Metabolism; Male; Middle Aged; Pancreas; Pancreatic Diseases; Protein-Energy Malnutrition; Proteins; Secretin; Starch; Trypsin

Topics: Amylases; Breath Tests; Carbon Dioxide; Cholecystokinin; Chymotrypsin; Diet; Feces; Glucose Tolerance Test; Humans; Intestinal Absorption; Lipase; Lipids; Pancreas; Pancreatic Diseases; Pancreatic Juice; Radionuclide Imaging; Secretin; Selenomethionine; Tolbutamide

Topics: Amino Acid Sequence; Aminopeptidases; Amylases; Animals; Carboxypeptidases; Cholecystokinin; Chymotrypsin; Deoxyribonucleases; Endopeptidases; Glucagon; Glucose Tolerance Test; Humans; Insulin; Lipase; Pancreas; Pancreatic Diseases; Pancreatic Elastase; Ribonucleases; Secretin; Tolbutamide; Trypsin

Topics: Aminopeptidases; Amylases; Cholecystokinin; Chymotrypsin; Deoxyribonucleases; Fatty Acids; Feces; Glucose Tolerance Test; Humans; Intestinal Secretions; Isoenzymes; Lipase; Lipids; Pancreas; Pancreatic Diseases; Pancreatic Juice; Secretin; Trypsin

In spite of having been the object of a number of studies, the association of morphologic and functional alterations of the pancreas with liver cirrhosis is as yet controversial. Therefore, the authors have studied exocrine pancreatic function in 40 patients: 8 with alcoholic cirrhosis, 18 with non-alcoholic cirrhosis, and 14 without evidence of hepatobiliary and pancreatic pathology. Pancreatic function was studied by the fecal chymotrypsin test which is sufficiently sensitive and specific and has been preferred in view of its practicability and non-invasiveness. Analysis of the results showed pathologic values to be significantly more frequent in subjects with alcoholic cirrhosis (50%, p < 0.05) compared to non-alcoholic cirrhotics (11.11%) and to controls (7.2%). These findings go to show that pancreatic exocrine deficit is frequently associated with alcoholic cirrhosis, thus confirming what has already been known about the pathogenetic role of alcohol which is apt to provoke both hepatic and pancreatic damage. Finally, it should be pointed out that pancreatic exocrine deficit is a purely functional alteration without clinical manifestations.

Topics: Aged; Chymotrypsin; Exocrine Pancreatic Insufficiency; Feces; Female; Humans; Liver Cirrhosis; Liver Cirrhosis, Alcoholic; Male; Middle Aged; Pancreatic Diseases; Pancreatic Function Tests

Crude preparations of hog gastric intrinsic factor or their own previously collected gastric juices administered with labeled vitamin B12 did not enhance vitamin B12 absorption in patients with vitamin B12 malabsorption secondary to pancreatic insufficiency. However, when these sources of gastric intrinsic factor were incubated with three times crystallized preparations of insolubilized bovine trypsin or chymotrypsin, the proteolytic enzymes were removed by centrifugation, and the preparations of gastric intrinsic factor were readministered to these patients, the absorption of vitamin B12 was markedly enhanced. Studies of hog gastric intrinsic factor before and after exposure to proteolytic enzymes failed to show any difference on Sephadex chromatography or polyacrylamide gel electrophoresis or on its affinity for vitamin B12 or the ileal receptor in guinea pigs. These investigations demonstrate that: (1) gastric intrinsic factor as secreted by subjects with pancreatic insufficiency or obtained from hog pyloric mucosal extracts is ineffective in promoting vitamin B12 absorption in patients with pancreatic insufficiency, (2) incubation of crude preparations of gastric intrinsic factor with insolubilized pancreatic proteases modified these preparations of gastric intrinsic factor in an as yet undefined manner, allowing them to enhance vitamin B12 absorption, and (3) in vitro studies using gut sacs or brush border preparations do not reflect the abnormality in vitamin B12 absorption associated with pancreatic dysfunction.

Topics: Anemia, Pernicious; Animals; Chymotrypsin; Clinical Trials as Topic; Female; Gastric Juice; Guinea Pigs; Humans; Intestinal Absorption; Intrinsic Factor; Pancreatic Diseases; Pancreatic Juice; Peptide Hydrolases; Swine; Trypsin; Vitamin B 12 Deficiency

Topics: Adult; Aged; Celiac Disease; Cholecystokinin; Chymotrypsin; Clinical Trials as Topic; Colonic Diseases, Functional; Feces; Female; Humans; Male; Middle Aged; Pancreas; Pancreatic Diseases; Secretin

Rare pathogenic variants in the SPINK1, PRSS1, CTRC, and CFTR genes have been strongly associated with a risk of developing chronic pancreatitis (CP). However, their potential impact on the age of disease onset and clinical outcomes, as well as their potential interactions with environmental risk factors, remain unclear. These issues are addressed here in a large Chinese CP cohort.. We performed targeted next-generation sequencing of the four CP-associated genes in 1061 Han Chinese CP patients and 1196 controls. To evaluate gene-environment interactions, the patients were divided into three subgroups, idiopathic CP (ICP; n = 715), alcoholic CP (ACP; n = 206), and smoking-associated CP (SCP; n = 140). The potential impact of rare pathogenic variants on the age of onset of CP and clinical outcomes was evaluated using the Kaplan-Meier model.. We identified rare pathogenic genotypes involving the SPINK1, PRSS1, CTRC, and/or CFTR genes in 535 (50.42%) CP patients but in only 71 (5.94%) controls (odds ratio = 16.12; P < 0.001). Mutation-positive patients had significantly earlier median ages at disease onset and at diagnosis of pancreatic stones, diabetes mellitus and steatorrhea than mutation-negative ICP patients. Pathogenic genotypes were present in 57.1, 39.8, and 32.1% of the ICP, ACP, and SCP patients, respectively, and influenced age at disease onset and clinical outcomes in all subgroups.. We provide evidence that rare pathogenic variants in the SPINK1, PRSS1, CTRC, and CFTR genes significantly influence the age of onset and clinical outcomes of CP. Extensive gene-environment interactions were also identified.

Topics: Adolescent; Adult; Age of Onset; Asian People; Calculi; Chymotrypsin; Cystic Fibrosis Transmembrane Conductance Regulator; Diabetes Mellitus; Gene-Environment Interaction; Genetic Predisposition to Disease; Genotype; Humans; Kaplan-Meier Estimate; Middle Aged; Mutation; Pancreatic Diseases; Pancreatitis, Alcoholic; Pancreatitis, Chronic; Smoking; Steatorrhea; Trypsin; Trypsin Inhibitor, Kazal Pancreatic; Young Adult

The faecal enzymes elastase and chymotrypsin are a relatively inexpensive non-invasive means of investigating causes of malabsorption. However, such tests may be affected by enzyme degradation or faecal dilution.. Faecal elastase-1 and chymotrypsin were measured in 225 patients in whom pancreatic disease was suspected, and the association between faecal free water and pH with these faecal enzymes was examined in subjects with normal pancreatic function.. The sensitivity of faecal elastase-1 and chymotrypsin for identifying exocrine pancreatic disease was 75% and 60%, respectively. Corresponding specificities for excluding disease were 95% and 97%. The positive predictive value for faecal elastase-1 increased from 58% to 92% when watery diarrhoea was excluded. Faecal elastase-1 (inversely) and chymotrypsin (directly) were significantly associated with percentage faecal free water content in subjects without pancreatic disease. Faecal elastase-1 was not related to faecal pH, whereas chymotrypsin was inversely related to pH.. Faecal elastase-1 is a more sensitive test for exocrine pancreatic disease in adults but is affected by dilution in patients with watery diarrhoea. The value of faecal chymotrypsin is limited by intestinal degradation.

Topics: Adult; Chymotrypsin; Enzyme-Linked Immunosorbent Assay; Feces; Gastrointestinal Diseases; Humans; Hydrogen-Ion Concentration; Pancreatic Diseases; Pancreatic Elastase; Predictive Value of Tests; Sensitivity and Specificity

Nutrient malabsorption frequently occurs in HIV infected children, but very few studies have investigated exocrine pancreatic digestive capacity in these cases.. To investigate pancreatic function in HIV infected children and to determine whether faecal fat loss, a prominent feature of intestinal dysfunction, is associated with pancreatic dysfunction.. Forty seven children with HIV infection without apparent pancreatic disease and 45 sex and age matched healthy controls.. Pancreatic function was evaluated by measuring elastase 1 concentration and chymotrypsin activity in stools by ELISA and colorimetric methods, respectively. Intestinal function was evaluated by measuring fat and protein loss by the steatocrit method and by faecal alpha1 antitrypsin concentration.. 14 (30%) had abnormal pancreatic function tests: seven had isolated elastase activity deficiency, three isolated chymotrypsin deficiency, and four pancreatic deficiencies in both enzymes. Patient enzyme values were significantly lower than those of controls. Low faecal pancreatic enzymes were not associated with symptoms. Twelve children had steatorrhoea and four had increased alpha1 antitrypsin. Steatorrhoea was significantly associated with reduced faecal pancreatic enzymes. There was a significant negative correlation between elastase 1 concentration and steatocrit. Children with pathological faecal elastase 1 or chymotrypsin values did not differ from the other HIV infected children with respect to nutritional and immunological status, stage of HIV disease, presence of opportunistic infections, or drug administration.. Abnormal pancreatic function tests are a frequent feature of paediatric HIV infection; this condition is associated with steatorrhoea, which probably contributes to the disease.

Topics: Adolescent; Case-Control Studies; Celiac Disease; Child; Child, Preschool; Chymotrypsin; Dietary Fats; Enzyme-Linked Immunosorbent Assay; Feces; Female; HIV Infections; Humans; Infant; Intestinal Absorption; Malabsorption Syndromes; Male; Pancreatic Diseases; Pancreatic Elastase; Prospective Studies

The determination of faecal pancreatic elastase 1 is a reliable test for the diagnosis of chronic pancreatic diseases in man due to its high sensitivity and specificity (93%). A clinical study was performed to investigate the detectability of canine faecal pancreatic elastase with polyclonal anti human pancreatic elastase 1 antibodies in 52 dogs with chronic diarrhoea and weight loss. To assess the diagnostic value of this parameter for the diagnosis of exocrine pancreatic insufficiency (EPI) in dogs faecal chymotrypsin activity was determined and serum trypsin-like immunoreactivity (TLI) concentration was measured within the Ceruletid test in all patients. The study revealed that canine faecal pancreatic elastase cross reacts with polyclonal anti human pancreatic elastase 1 antibodies. In comparison with the results of the other pancreas tests it was proved that the concentration of canine faecal pancreatic elastase determined by rocket immunoelectrophoresis is highly sensitive for EPI in dogs (sensitivity 100%) but there are species differences in specificity between man and dog (specificity 56.5%).

Topics: Animals; Antibodies; Chronic Disease; Chymotrypsin; Diarrhea; Dog Diseases; Dogs; Feces; Humans; Immunoelectrophoresis; Pancreatic Diseases; Pancreatic Elastase; Predictive Value of Tests; Sensitivity and Specificity; Trypsin; Weight Loss

During a secretin-cerulein test for exocrine pancreatic function, venous acid-base analysis was performed before and 30 and 45 min after the intravenous injection of secretin (1 clinical unit/kg body weight). A decrease in plasma bicarbonate was observed in persons with normal exocrine pancreatic function as defined by normal bicarbonate and enzyme secretion in the secretin-cerulein test (n = 39). Bicarbonate values were 94.8 +/- 3.6% (mean +/- SD) of the initial concentration after 30 min and 92.9 +/- 3.9% after 45 min. In contrast, there was no statistically significant decrease in plasma bicarbonate in patients with global pancreatic exocrine deficiency (n = 15). In normal exocrine pancreatic function, the maximal plasma bicarbonate decrease was 2.17 +/- 1.12 mM (mean +/- SD; n = 39). In patients with global exocrine deficiency, however, a maximal plasma bicarbonate decrease of 0.54 +/- 0.68 mM (n = 15) was obtained. The difference was highly significant (p < 0.001). In patients with partial exocrine deficiency (isolated decrease in bicarbonate secretion or reduced excretion of a single enzyme), values were also significantly lower (1.44 +/- 1.40 mM; n = 14; p < 0.05). The maximal plasma bicarbonate decrease correlated with the bicarbonate secretion into the duodenal juice (r = 0.62, p < 0.001). If a maximal plasma bicarbonate decrease > or = 0.9 mM was considered normal, determination of plasma bicarbonate following secretin administration allowed us to detect the presence of global exocrine deficiency with a sensitivity of 87% and a specificity of 87%. The secretin-induced plasma bicarbonate decrease may therefore be used as a new simple tubeless test to evaluate exocrine pancreatic function.

Topics: Acid-Base Equilibrium; Amylases; Bicarbonates; Ceruletide; Chymotrypsin; Female; Humans; Kinetics; Lipase; Male; Pancreas; Pancreatic Diseases; Secretin; Trypsin

To compare the pancreatic exocrine and beta-cell function in the two variants of malnutrition-related diabetes mellitus (MRDM): fibrocalculous pancreatic diabetes (FCPD) and protein-deficient pancreatic diabetes (PDPD).. Fecal chymotrypsin (FCT) and fasting C-peptide levels were measured in 20 consecutive patients with FCPD and 19 with PDPD. FCPD was diagnosed by pancreatic calcification on ultrasonography, while the diagnosis of PDPD was made on the basis of low body mass index, severe diabetes requiring insulin therapy, and ketosis resistance on interruption of insulin. Twenty patients with type I diabetes and 32 healthy subjects served as control subjects.. Both FCPD and PDPD patients had diminished levels of FCT when compared with those of control subjects and patients with type I diabetes. However, FCT levels were significantly lower in subjects with FCPD (median 0.4 U/g, range 0-8.9 U/g), in comparison with those with PDPD (4.7 U/g, 0.6-40.5 U/g; P < 0.001). Of the FCPD patients, 13 of 20 (65%) had severe exocrine pancreatic deficiency (FCT < 1 U/g) vs. 3 of 19 (15.8%) PDPD subjects (P < 0.01). In comparison with control subjects, fasting serum C-peptide levels were significantly diminished in both MRDM groups. However, C-peptide levels in subjects with FCPD (mean +/- SE, 0.22 +/- 0.04 nmol/l) and PDPD (0.26 +/- 0.04 nmol/l) were comparable.. Among the two variants of MRDM, subjects with FCPD have severe pancreatic exocrine deficiency in comparison with those with PDPD, even though their C-peptide levels are comparably diminished. This suggests that the pathogenesis of these two entities may differ or that the genetic and/or environmental factors leading to exocrine damage are different.

Topics: Adult; Blood Glucose; Body Mass Index; C-Peptide; Chymotrypsin; Diabetes Mellitus; Diabetes Mellitus, Type 1; Feces; Female; Glycated Hemoglobin; Humans; India; Insulin; Insulin Secretion; Islets of Langerhans; Male; Nutrition Disorders; Pancreas; Pancreatic Diseases; Reference Values; Statistics, Nonparametric

Serum pancreatic enzyme behavior, exocrine function, and morphology of the pancreas were studied in 28 patients with end-stage renal disease undergoing regular hemodialysis, in order to better delineate and assess the clinical relevance of the pancreatic alterations that occur in these patients. Twenty-eight healthy subjects served as controls. Initial studies included serum amylase, isoamylase, and lipase assays; fecal chymotrypsin measurement; and abdominal ultrasonography. The amylase, lipase, and chymotrypsin determinations, as well as ultrasound examination, were repeated four years later. None of the patients had clinical evidence of pancreatic disease at entry into the study, but one had had previous attacks of pancreatitis and another developed mild acute pancreatitis one month after entry. Initial mean serum enzyme levels were significantly higher in patients than in controls (amylase, pancreatic isoamylase, and lipase, P < 0.001; salivary isoamylase P < 0.05). Serum amylase was raised in 16/28 patients; pancreatic isoamylase in 15/28, and lipase in 7/28; these elevations were generally mild. Mean fecal chymotrypsin was significantly lower (P < 0.001) in patients than in controls: abnormally low values were found in 9/28 patients. Amylase, lipase and chymotrypsin measurements repeated after four years showed no significant difference with respect to the first study. Ultrasonographic changes were rare and mild: one patient had a small cyst in the pancreas head, another, an increase in echogenicity of the gland not related to age; these findings were unchanged at repeat examination. The results demonstrate that the frequent elevations of serum pancreatic enzymes and the rare sonographic changes found in patients undergoing hemodialysis do not generally reflect a relevant pancreopathy. However, the finding of significantly decreased fecal chymotrypsin may indicate the presence of pancreatic dysfunction in end-stage renal disease.

Topics: Amylases; Case-Control Studies; Chymotrypsin; Clinical Enzyme Tests; Feces; Female; Follow-Up Studies; Humans; Isoenzymes; Kidney Failure, Chronic; Lipase; Male; Middle Aged; Pancreas; Pancreatic Diseases; Pancreatitis; Renal Dialysis; Time Factors; Ultrasonography

Topics: Administration, Oral; Adult; Ascites; Chymotrypsin; Humans; Male; Pancreatic Diseases; Pancreatic Juice; Pleural Effusion; Trypsin

Topics: Adult; Aged; Chymotrypsin; Feces; Female; Histamine H2 Antagonists; Humans; Male; Middle Aged; Pancreatic Diseases

1. The pancreatic digestive enzyme activities of trypsin and chymotrypsin were assessed in vitro and were found to correlate well with the histological changes characteristic of pancreas disease (PD) in farmed Atlantic salmon (Salmo salar). 2. Pancreatic enzyme activity was assessed in vivo using the chymotrypsin specific substrate N-benzoyl-L-tyrosyl-p-aminobenzoic acid. In all cases, significantly less p-aminobenzoic acid was excreted by fish later found to be suffering from PD. 3. It is concluded that the in vitro digestive enzyme assay was effective in diagnosing PD with the in vivo method, indicating further promise for assessing exocrine pancreatic function.

Topics: Animals; Chymotrypsin; Fish Diseases; Pancreatic Diseases; Salmon; Trypsin

The exocrine pancreas produces many of the enzymes responsible for the digestion of food. Severe alterations in exocrine pancreas function cause malabsorption which predominantly affects fats. Unfortunately, because it is a deep organ the pancreas is a difficult target for investigations. A large number of diagnostic tests have been developed to gather information on pancreatic function with minimal invasiveness. Although helpful in everyday practice, each of these methods investigates only one of the multiple components of pancreatic secretory function and all are relatively insensitive, i.e., detect only severe secretion deficiencies. Furthermore, none of these tests can evaluate water and electrolyte secretion. Consequently, invasive duodenal juice studies with stimulation remain the "gold standard" for evaluating exocrine pancreas function.

Topics: 4-Aminobenzoic Acid; Chymotrypsin; Feces; Fluoresceins; Humans; Pancreatic Diseases; Pancreatic Function Tests; Sensitivity and Specificity

Topics: 4-Aminobenzoic Acid; Amylases; Caprylates; Chymotrypsin; Feces; Humans; Isoamylase; Pancreatic Diseases; Pancreatic Function Tests; para-Aminobenzoates; Secretin; Triglycerides

Twenty adult patients affected by atopic dermatitis (AD) were submitted to the p-aminobenzoic acid (PABA) test in order to evaluate the proteolytic pancreatic function. All but one showed a normal PABA test. These results seem to exclude a proteolytic maldigestion as a pathogenetic factor in AD.

Topics: 4-Aminobenzoic Acid; Adult; Chymotrypsin; Dermatitis, Atopic; Female; Food Hypersensitivity; Humans; Immunoglobulin E; Male; Pancreatic Diseases; Severity of Illness Index

This study was performed to assess the effects of misoprostol, a synthetic prostaglandin E1 analog, on cerulein-induced pancreatitis. Per group of 10 each, male Wistar rats received either cerulein (2.5 micrograms/kg/h subcutaneously), cerulein and misoprostol (500 micrograms/kg intraperitoneally at 0 and 4 h), or saline. Rats were killed 6 h after the first injection. Misoprostol treatment significantly reduced interstitial edema and acinar cell lesions induced by hyperstimulation. Pancreatic amylase and chymotrypsin contents were increased by cerulein and returned towards control levels in the misoprostol-treated group. The lysosomal volume density and the pancreatic beta-D-glucuronidase activity were significantly increased after hyperstimulation. The two parameters were significantly reduced by misoprostol. A protective effect of misoprostol against lesions induced by cerulein hyperstimulation would be a consequence of a lysosomal stabilizating effect.

Topics: Acid Phosphatase; Acute Disease; Alprostadil; Amylases; Animals; Ceruletide; Chymotrypsin; Edema; Glucuronidase; Male; Microscopy, Electron; Misoprostol; Organ Size; Pancreatic Diseases; Pancreatitis; Prostaglandins E, Synthetic; Rats; Rats, Inbred Strains

Exocrine pancreatic function was studied by fecal chymotrypsin test in three groups of diabetic patients seen in southern India. Exocrine pancreatic insufficiency, as shown by low fecal chymotrypsin levels, was seen in 87.5% of patients with fibrocalculous pancreatic diabetes (FCPD), in 23.5% of insulin-dependent diabetes mellitus patients, and in 4.5% of non-insulin-dependent diabetes mellitus patients. There was no correlation between fecal chymotrypsin levels and serum amylase, serum lipase, age, body mass index, duration of diabetes, fasting plasma glucose, or glycosylated hemoglobin levels. The fecal chymotrypsin test is a useful additional investigation for the diagnosis of FCPD found in tropical countries.

Topics: Adult; Amylases; Blood Glucose; Chymotrypsin; Diabetes Mellitus, Type 1; Feces; Female; Glycated Hemoglobin; Humans; Lipase; Male; Pancreas; Pancreatic Diseases; Reference Values

Topics: Chymotrypsin; Feces; Humans; Pancreatic Diseases; Radioimmunoassay; Reference Values; Specimen Handling

Topics: 4-Aminobenzoic Acid; Aminobenzoates; Chymotrypsin; Feces; Humans; Pancreatic Diseases; Pancreatic Function Tests; para-Aminobenzoates; Postoperative Period

Using a new colorimetric method we measured the faecal chymotrypsin in 407 subjects, divided as follows: 252 adult subjects with a normal exocrine pancreatic function as shown by duodenal intubation, 24 adult patients with a mild to moderate pancreatic insufficiency, and 26 adult patients with severe pancreatic insufficiency. In addition, 40 healthy children, 50 children with chronic diarrhoea, and 15 with cystic fibrosis were studied before and after substituting enzyme therapy. Faecal chymotrypsin was found to be useful in evaluating the degree of exocrine functional insufficiency in subjects with diseases of the pancreas that had already been clinically ascertained. The same cannot be said for its ability to provide an early diagnosis of subjects with a slight-moderate insufficiency in exocrine pancreatic function.

Topics: Adult; Child; Chymotrypsin; Colorimetry; Feces; Humans; Pancreas; Pancreatic Diseases; Pancreatic Function Tests

An in-vitro test of degradation of haptocorrin, a cobalamin-binding glycoprotein, was used to diagnose exocrine pancreatic dysfunction. This radioisotopic test (TDH) required only 50 microliters duodenal juice collected during endoscopy after stimulation with 1 U/kg secretin intravenously. The initial reaction mixture, composed of salivary haptocorrin saturated with cobalt-57-labelled cyanocobalamin and unsaturated intrinsic factor, was incubated with 25 microliters duodenal juice. The percentage of degraded haptocorrin was estimated from the proportion of labelled cyanocobalamin that was transferred from haptocorrin to intrinsic factor. The TDH result was 41.6 +/- 31.7% (SD) in a group of chronic pancreatitis patients (n = 22) and 91.5 +/- 4.8% in the control group (n = 47). The sensitivity and specificity for exocrine pancreatic dysfunction were estimated as 0.91 and 0.96, respectively, for a lower limit of normal values of 81.7%. A hyperbolic relation was found between the TDH and the trypsin or chymotrypsin activity in duodenal juice (p less than 0.001). In this study, the N-benzoyl-tyrosyl-p-aminobenzoic acid test was less sensitive than the TDH, since its result was abnormal in only 64% of the patients. The TDH was easier to carry out and less time-consuming than the determination of pancreatic enzyme output in duodenal juice collected after hormonal stimulation.

Topics: Adult; Aged; Chymotrypsin; Duodenum; Humans; Intestinal Secretions; Middle Aged; Pancreatic Diseases; Pancreatic Function Tests; Transcobalamins; Trypsin

The aim of this study was to assess the analytical performance of the BMC stool chymotrypsin test and its accuracy in diagnosing pancreatic disease in infants. The test utilizes a detergent which solubilizes chymotrypsin bound to stool residues, and a tetrapeptide coupled to p-nitroaniline which is specifically cleaved by chymotrypsin. We employed the IL Multistat at 30 degrees C to monitor enzyme activity as an increase in absorbance at 405 nm. The reaction was linear to 600 U/g stool. Recovery of exogenous chymotrypsin with a single detergent extraction was 98-105%, and of endogenous chymotrypsin (as determined by multiple extractions) 80-97%. Imprecision (CV) was 2.2% within-day and 2.4% between-day for the BMC control, and 2.4-5.2% for stool chymotrypsin in the range 8.3-14.4 U/g. Since the test utilises only 100 mg of stool, inhomogeneity of enzyme distribution was assessed by multiple assays on a single stool, which revealed a range of activity from 4.2-150%. We therefore recommend sampling of each stool in triplicate. With this procedure, chymotrypsin was measured in 220 consecutive stool samples submitted for fat determination from children. Applying the manufacturer's lower reference limit of 4.1 U/g, the following results were obtained (number abnormal/total number): suspected intestinal disease with normal stool fat (5/127); proven intestinal disease and increased stool fat (1/26); untreated cystic fibrosis (CF) with (19/22), and without (0/3) steatorrhea; CF with pancreatic insufficiency on replacement therapy (4/42).(ABSTRACT TRUNCATED AT 250 WORDS)

Topics: Chymotrypsin; Cystic Fibrosis; Fats; Feces; Humans; Infant; Malabsorption Syndromes; Pancreatic Diseases; Photometry

Topics: Adolescent; Adult; Child; Child, Preschool; Chymotrypsin; Feces; Female; Humans; Male; Middle Aged; Pancreatic Diseases; Reagent Kits, Diagnostic

Topics: Chymotrypsin; Diarrhea; Esters; Exocrine Pancreatic Insufficiency; Feces; Humans; Pancreatic Diseases; Photometry; Tyrosine

We measured the distribution of chymotrypsin within feces by comparing duplicate 100-mg stool aliquots from 48 stool specimens. For practical purposes, the distribution of the enzyme in stool appears sufficiently homogeneous to assure representative results even from 100-mg stool aliquots. Given this likelihood, we have developed a new disposable device that measures 100-mg stool aliquots hygienically, prepares this material for shipping by mail, homogenizes and suspends the stool sample, and facilitates centrifugation of the fecal suspension, all within the same instrument. Performance studies with this new device revealed that stools of different consistency can be measured out precisely and conveniently by volume. The difference in the specific weight of different stools appears to be so low that for practical purposes a 100-mg mass of stool can be weighed out by volume.

Topics: Centrifugation; Chymotrypsin; Feces; Humans; Pancreatic Diseases; Specimen Handling; Spectrophotometry; Suspensions

Assessment of the clinical value of the pancreolauryl test (PLT) in the literature range from "useless" to a specifity of 95% and a sensitivity of 98%. In this work, our own data are presented in relation to various reference methods. The results are derived from the largest collective investigated to data, comprising 40 controls and 391 patients (108 with chronic pancreatitis and 283 with other gastrointestinal disorders). The specifity of the the PLT varies between 81% and 95% according to the "quality" of the control collective. The PLT is particularly frequently pathological in patients with diseases in the region of the gallbladder/bile duct and the gastrointestinal tract. The sensitivity of the PLT for chronic pancreatitis varies between 68% and 100%, depending on 9 different reference methods employed. Based on the prevalence of chronic pancreatitis with exocrine insufficiency in various patient collectives, the predictive value of the PLT for the presence of this disorder can be calculated using our data.

Topics: Cholangiopancreatography, Endoscopic Retrograde; Cholecystokinin; Cholelithiasis; Chronic Disease; Chymotrypsin; Diagnosis, Differential; Exocrine Pancreatic Insufficiency; Gastrointestinal Diseases; Humans; Liver Diseases; Pancreatic Diseases; Pancreatic Function Tests; Pancreatitis; Secretin; Tomography, X-Ray Computed

Pancreas divisum was demonstrated in 22 of 500 consecutive ERCP (4.4%). Among patients with otherwise normal ERCP, pancreas divisum was found in 12.8%. In contrast, only 1.8% of patients with other pathology in the ERCP exhibited pancreas divisum (p less than 0.001). In relation to the clinical indication, pancreas divisum was found in 13.3% of patients with suspected or proven pancreatitis, in 1.9% of patients with suspicion of biliary tract disease (p less than 0.001), in 1.9% of patients with suspicion of pancreatic cancer (p less than 0,05) and in 4.4% of patients with epigastric pain of undetermined origin (p greater than 0.05). In 14 patients pancreas divisum was the only pathological finding in a thorough clinical and gastrointestinal workup; 6 of the 14 patients had had typical episodes of pancreatitis, in 6 other patients there was clinical and biochemical evidence of pancreatic disease (mainly pain and hyperenzymemia), and the last 2 cases had chronic epigastric pain without biochemical abnormalities. In 2 patients of this series the pancreas divisum was misinterpreted morphologically (sonography, autopsy) as tumor of the head of the pancreas. Based upon our experience and the literature, the following practical conclusions can be drawn: 1. Pancreas divisum may cause typical episodes of acute (relapsing) pancreatitis. 2. In patients with chronic epigastric pain associated with hyperenzymemia but without typical acute pancreatitis, pancreas divisum may be the cause. 3. Morphologically pancreas divisum may mimic a pancreatic tumor (sonography, computer-tomography, autopsy).

Topics: Abdomen; Adult; Aged; Amylases; Cholangiopancreatography, Endoscopic Retrograde; Chymotrypsin; Feces; Female; Humans; Lipase; Male; Middle Aged; Pain; Pancreas; Pancreatic Diseases; Pancreatitis

A radioimmunoassay for human pancreatic chymotrypsin II has been developed. Serum immunoreactive chymotrypsin II content in healthy individuals ranged from 14.7 ng/ml to 77.5 ng/ml, the average being 37.5 ng/ml (SD = 19.6). Elevated values were observed in patients with acute pancreatitis and renal failure. After total pancreatectomy, serum immunoreactive chymotrypsin II was not detectable. A significant positive correlation was observed between serum immunoreactive chymotrypsin II and cationic trypsin contents.

Topics: Antibody Specificity; Chymotrypsin; Humans; Kidney Failure, Chronic; Pancreas; Pancreatic Diseases; Radioimmunoassay; Stomach Neoplasms

Topics: Chymotrypsin; Feces; Humans; Pancreatic Diseases; Pancreatic Neoplasms; Pancreatitis

Pancreozymin-secretin tests were carried out in children aged from 0,5 till 12 years by means of a two lumen tube of the Salem-Sump-type and a three lumen perfusion tube. For stimulation we used 2 U/kg of the hormones, each from BOOTs-Corp. Amylase was determined with dinitrosalicylic acid, lipase by titration of acidic equivalents after half hour incubation and trypsin and chymotrypsin with TAME and BTEE respectively. We used PEG 4000 as marker and quantified enzymes secretion as well as liquid secretion by it. We got up to 50% lower results by testing with the two lumen tube. If we are laying the perfusion tube we measured an elevation of the two lumen tube. If we are laying the perfusion tube we measured an elevation of the II-hydroxycorticoides. The concentration of the enzymes in the specimines before perfusion on 3 consecutive days fell by 90% on the average. We discussed some problems of the determination of enzymes and performing of the tests by means of the results.

Topics: Amylases; Child; Child, Preschool; Chymotrypsin; Humans; Infant; Lipase; Pancreas; Pancreatic Diseases; Pancreatic Function Tests; Trypsin

In many ways diagnosis of pancreatic disorders in children is difficult. Since pancreatic parameters are age-dependent, reliable laboratory parameters are not easily established. Children are less likely than adults to endure tolerance tests and invasive test methods should therefore be used only in special situations. Estimation of chymotrypsin in faeces seems to be an earlier indicator of pancreatic insufficiency than the PABA-peptide-test. A secretin-pancreozymin test can only be advised for first diagnosis after screening has repeatedly indicated pathological values and malabsorption has more or less been ruled out. A threefold rise in serum amylase values - matched for age - suggests pancreatitis and sonography should then be applied to obtain further clarification.

Topics: 4-Aminobenzoic Acid; Age Factors; Amylases; Child; Child, Preschool; Cholecystokinin; Chymotrypsin; Exocrine Pancreatic Insufficiency; Feces; Humans; Infant; Infant, Newborn; Pancreatic Diseases; Pancreatitis; Secretin

Topics: 4-Aminobenzoic Acid; Administration, Oral; Aminobenzoates; Chymotrypsin; Humans; Pancreatic Diseases; Pancreatic Function Tests; para-Aminobenzoates; Tyrosine

The pancreas can be studied for obstructive disease by measuring serum lipase levels in the two stage provocative test. The test is nonspecific but noninvasive and applicable to all stages of pancreatic diseases. In this test, the pancreas is stimulated twice in two hour intervals before measuring the serum enzyme levels: first, with pancreozyin and secretin--the stage 1 test and, second, with pancreozymin, secretin, betazole hydrochloride and morphine sulfate--the stage 2 test. Among the pancreatic enzymes measured, lipase was most reliable. Serum lipase level elevation in the stage 1 test indicates a pancreatic abnormality and it completes the test. Patients who fail to respond to the stage 1 test have either a normal pancreas or pancreatic insufficiency and need the stage 2 test for differential diagnosis. In the stage 2 test, the serum lipase level is elevated in patients with a normal pancreas but not in those with pancreatic insufficiency. As a preliminary study, ten patients with carcinoma of the pancreas, two with pancreatitis and ten in the control group were studied. All patients with a known pancreatic disease demonstrated an abnormality in the test. Two of ten in the control group also had abnormal results. The two stage provocative test may be used prior to undertaking more invasive examinations, such as an arteriogram, in patients who are suspected of having pancreatic disease, yet other tests have failed to indicate it.

Topics: Amylases; Betazole; Cholecystokinin; Chymotrypsin; Clinical Enzyme Tests; Female; Humans; Lipase; Male; Morphine; Pancreatic Diseases; Pancreatic Neoplasms; Pancreatitis; Secretin; Trypsin

Topics: Adult; Amylases; Carboxypeptidases; Chronic Disease; Chymotrypsin; Clinical Enzyme Tests; Deoxyribonucleases; Humans; Lipase; Liver Cirrhosis; Pancreas; Pancreatic Diseases; Pancreatic Neoplasms; Pancreatitis; Ribonucleases; Trypsin

Topics: Chymotrypsin; Clinical Enzyme Tests; Colitis; Colon, Sigmoid; Crohn Disease; Diagnosis, Differential; Feces; Humans; Pancreatic Diseases; Proctocolitis; Trypsin

An indirect exocrine pancreatic function test (PFT) which measures the ability of a test to hydrolyze a chymotrypsin-labile peptide (N-benzoyl-L-tyrosyl-PABA), was carried out in rats and swine with simulated partial exocrine pancreatic insufficiency. When spray-dried egg white (SDEW), which contains an inhibitor of chymotrypsin, was administered as a test meal with the PFT, the degree of pancreatic insufficiency was more pronounced. The results suggest that SDEW or raw egg while may be useful as a test meal to be given in conjunction with the PFT in humans in order to accentuate moderate degrees of pancreatic insufficiency and improve the sensitivity of this indirect test of pancreatic function.

Topics: 4-Aminobenzoic Acid; Amines; Aminobenzoates; Animals; Caseins; Chymotrypsin; Diet; Dogs; Egg White; Female; Male; Methods; Pancreas; Pancreatic Diseases; Pancreatin; Peptides; Rats; Swine

The synthetic peptide N-benzoyl-L-tyrosyl-p-amino-benzoic acid is selectively metabolized by chymotrypsin. Its derivates are excreted in urine and are taken as a measure of exocrine pancreatic insufficiency. The results of PABA-peptide test, of chymotrypsin activity and of the fat content of faeces were compared with each others in 25 patients suspicious to exocrine pancreatic insufficiency. The results correlate well. Because of the practicability the PABA-peptide test is suggested as an additional routine-method in diagnosis of pancreatic functions although it does not substitute any established method.

Topics: 4-Aminobenzoic Acid; Aminobenzoates; Chymotrypsin; Feces; Humans; Lipids; Pancreatic Diseases

Topics: 4-Aminobenzoic Acid; Adult; Aminobenzoates; Chymotrypsin; Female; Humans; Male; Middle Aged; Pancreatic Diseases; Pancreatin; para-Aminobenzoates; Tyrosine

Topics: 4-Aminobenzoic Acid; Amylases; Chymotrypsin; Duodenum; Feces; Humans; Intestinal Secretions; Methods; Pancreas; Pancreatic Diseases; Peptides

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

Cobalamin (Cbl; vitamin B(12)) malabsorption in pancreatic insufficiency can be partially corrected by bicarbonate and completely corrected by pancreatic proteases but the mechanisms involved are unknown. Because saliva contains enough R-type Cbl-binding protein (R protein) to bind all of the dietary and biliary Cbl, it is possible that R protein acts as an inhibitor of Cbl absorption and that pancreatic proteases are required to alter R protein and prevent such inhibition. To test this hypothesis we studied the ability of R protein and intrinsic factor (IF) to compete for Cbl binding and ability of pancreatic proteases to alter this competition. Human salivary R protein bound Cbl with affinities that were 50- and 3-fold higher than those of human IF at pH 2 and 8, respectively. Cbl bound to IF was transferred to an equal amount of R protein with t((1/2))'s of 2 and 90 min at pH 2 and 8, respectively, and within several hours respective ratios of R protein-Cbl/IF-Cbl of 50 and 2 were observed. Cbl bound to R protein was not transferred to IF at either pH 2 or 8. Incubation of R protein with pancreatic proteases at pH 8 led to a 150-fold decrease in its affinity for Cbl. Incubation of R protein-Cbl with pancreatic proteases led to complete transfer of Cbl to IF within 10 min. Gel filtration studies with R protein-[(57)Co]Cbl and (125)I-R protein showed that pancreatic proteases partially degraded R protein. Pancreatic proteases differed in their ability to effect these changes with trypsin > chymotrypsin > elastase. Pancreatic proteases did not alter IF in any of the parameters mentioned above. Pepsin failed to alter either R protein or IF. THESE STUDIES SUGGEST THE FOLLOWING: (a) that Cbl is bound almost exclusively to R protein in the acid milieu of the stomach, rather than to IF as has been assumed previously; (b) that Cbl remains bound to R protein in the slightly alkaline environment of the intestine until pancreatic proteases partially degrade R protein and enable Cbl to become bound exclusively to IF; and (c) that the primary defect in Cbl absorption in pancreatic insufficiency is a lack of pancreatic proteases and a failure to alter R protein and effect the transfer of Cbl to IF. These studies also suggest that the partial correction of Cbl malabsorption observed with bicarbonate is due to neutralization of gastric HCl, since at slightly alkaline, pH IF can partially compete with R protein for the initial binding and retention of Cbl.

Topics: Carrier Proteins; Chymotrypsin; Endopeptidases; Humans; Hydrogen-Ion Concentration; In Vitro Techniques; Intestinal Absorption; Intrinsic Factor; Pancreas; Pancreatic Diseases; Pancreatic Elastase; Pancreatin; Pepsin A; Proteins; Trypsin; Vitamin B 12

Topics: 4-Aminobenzoic Acid; Adult; Aged; Aminobenzoates; Chymotrypsin; Humans; Middle Aged; Pancreatic Diseases; Pancreatin; Pancreatitis; Peptides

The synthetic peptide N-benzoyl-L-tyrosyl-p-aminobenzoic acid is specifically cleaved by chymotrypsin to Bz-Ty and PABA. The liberated PABA is absorbed and excreted in the urine. Accordingly, PABA recovery reflects intraluminal chymotrypsin activity and is an index of exocrine pancreatic function. This test was evaluated in 24 patients with cystic fibrosis to determine its role in the diagnosis of exocrine pancreatic insufficiency. Cumulative percent PABA recovery in six hours was significantly lower in CF patients compared with the control group. No overlap was noted between the two groups. There was good correlation between PABA recovery, fecal chymotrypsin activity, and coefficient of fat absorption. These findings indicate that PABA recovery is significantly reduced in patients with CF and steatorrhea and may prove a practical and reliable test of pancreatic insufficiency.

Topics: 4-Aminobenzoic Acid; Adolescent; Adult; Aminobenzoates; Child; Child, Preschool; Chymotrypsin; Cystic Fibrosis; Feces; Humans; Lipids; Pancreatic Diseases; para-Aminobenzoates

Topics: 4-Aminobenzoic Acid; Chymotrypsin; Feces; Humans; Pancreatic Diseases; Peptides

P-Amino-benzoic acid (PABA) is split specifically by pancreatic chymotrypsin from the synthetic tripeptide N-benzoyl-L-tyrosyl-PABA. The urinary excretion of absorbed PABA serves as an index for exocrine pancreatic function. The peptide (0.015 g/kg) was administered orally to 20 controls (aged between 5 months and 16 years), 6 patients with exocrine pancreatic insufficiency caused by cystic fibrosis (CF), and 9 newborn infants. In the controls the mean 6-hour PABA recovery was 58.5% (+/- 11.2 SD). Recovery in patients with CF was lower (P less than 0.001) with no overlap. In newborn infants the mean 6-hour PABA recovery was 23.4 (+/- 17.7 SD); overlapping in 3 instances with the results in CF patients. This simple, noninvasive test thus appears promising and merits further investigation in younger infants, especially newborns.

Topics: 4-Aminobenzoic Acid; Adolescent; Aminobenzoates; Child; Child, Preschool; Chymotrypsin; Cystic Fibrosis; Female; Humans; Infant; Infant, Newborn; Male; Pancreas; Pancreatic Diseases

Topics: 4-Aminobenzoic Acid; Chymotrypsin; Feces; Humans; Pancreatic Diseases

Pancreatic ascites is a rare disease which is often misinterpreted as ascites secondary to alcoholic cirrhosis or to intraabdominal cancer. It can be diagnosed by a high protein and amylase/lipase content of the ascitic fluid. If diagnosis and subsequent surgery occur at an early stage, the prognosis is good. The natural course, therapy, prognosis, and pathogenesis of pancreatic ascites are discussed on the basis of experience with 7 patients.

Topics: Adolescent; Adult; Alcoholism; Amylases; Ascites; Ascitic Fluid; Chymotrypsin; Feces; Female; Humans; Male; Pancreatic Diseases; Pancreatitis; Proteins

Fecal chymotrypsin (CT) activities were determined in 149 randomly collected fecal specimens of 80 patients in whom the pancreatic function had been tested by a secretin-cholecystokinin test. There was a significant correlation between fecal CT activities and outputs of trypsin (r = 0.3451, p less than 0.01) and amylase (r = 0.3285, p less than 0.01) in duodenal juice. Fecal CT activities were normal in all patients who--based upon enzyme outputs in duodenal juice after stimulation with secretin and CCK/PZ--were classified as 'borderline cases', in most patients with 'low-normal' pancreatic function, and in a significant number of patients with established insufficiency of exocrine pancreas. On the other hand, fecal CT activities were abnormal in patients with severely impaired output of trypsin in duodenal juice, and only 7% of the fecal specimens from patients with established normal function of exocrine pancreas had abnormal low CT activities. It is concluded that the sensitivity of the fecal enzyme method is rather low as compared to the secretin-cholecystokinin test, but that fecal CT determinations give valuable diagnostic information in patients with more pronounced insufficiency of the exocrine pancreas.

Topics: Amylases; Cholecystokinin; Chymotrypsin; Duodenum; Feces; Humans; Pancreas; Pancreatic Diseases; Secretin; Trypsin

I assayed 16 commercially available pancreatic extracts (representing capsules, tablets and enteric-coated tablets) for enzyme activities and the relation between the in vitro activities and in vivo potency evaluated in man. Lipase activity ranged from 10 to 3600 units per unit, with 11 preparations containing less than 600 units per unit. The preparations with the highest lipase activities were llozyme, 3600, Kuzyme HP, 2330, Festal, 2073, Cotazym, 2014, and Viokase, 1636 units. Lipase activity in vitro correlated with potency in vivo for tablets and capsules, with tablets and capsules being effective in reducing steatorrhea by 56.1 +/- 9 per cent and 48.6 +/- 10 per cent (mean +/- S.E.M.) respectively, P less than 0.001. Enteric-coated tablets were less effective (20 +/- 13 per cent reduction, P greater than 0.02). The longer the gastric pH remained greater than or equal to 4 (r = 0.915, P less than 0.01) and the higher the average duodenal pH (r = 0.966, P less than 0.01), the more marked the reduction in steatorrhea.

Topics: Administration, Oral; Biological Availability; Capsules; Celiac Disease; Chronic Disease; Chymotrypsin; Duodenum; Feces; Female; Gastric Mucosa; Humans; Hydrogen-Ion Concentration; In Vitro Techniques; Lipase; Male; Nitrogen; Pancreas; Pancreatic Diseases; Pancreatic Extracts; Pancreatic Juice; Tablets; Tablets, Enteric-Coated

Premature activation of proteolytic zymogens (trypsinogen, chymotrypsinogen) as an early step in the pathogenesis of exocrine pancreatic insufficency (EPI) syndrome in CBA/J mice was investigated in electrophoresed pancreatic homogenates. Polyacrylamide gels containing extracts from control pancreas required prior activation of trypsinogen and chymotrypsinogen (with exogenously added enterokinase and trypsin, respectively) to produce activity staining with specific synthetic substrates. On the contrary, bands of activity staining in gels containing homogenates from mice with EPI syndrome could be readily detected without trypsin or enterokinase preincubation. Subcellular fractionation of control and diseased pancreas revealed that the premature intracellular proteolysis was confined to the zymogren granule fraction, which, even in very moderately affected pancreases (10 to 30% acinar cell autolysis), was very labile in vitro. These proteolytic events reflect the biochemical consequences of zymogen granule destabilization that were observed at the ultrastructural level.

Topics: Animals; Chemical Fractionation; Chymotrypsin; Chymotrypsinogen; Cytoplasmic Granules; Electrophoresis, Polyacrylamide Gel; Enzyme Precursors; Female; Male; Mice; Mice, Inbred CBA; Pancreatic Diseases; Rodent Diseases; Staining and Labeling; Trypsin; Trypsinogen

Topics: Chronic Disease; Chymotrypsin; Feces; Humans; Methods; Pancreatic Diseases

Fecal chymotrypsin activity was measured in 128 samples from 93 persons; the titrimetric procedure (Haverback) was used. Distribution of values in 67 normal persons was slanted positively and was approximatively logarithmical. The lower limit of normal was 120 microgram/g stool. Falsely normal results were obtained in 23% of 45 stool samples from 26 patients with pancreatic insufficiency. Falsely pathological results were found in 3,6% of cases. When chymotrypsin was measured photometrically (Imondi) and when the normal limit was assumed to be 50 microgram/g stool according to the literature, a diagnosis of pancreatic insufficiency was confirmed only in 30% of all patients, and 44% of the results were falsely pathological. Chymotrypsin was measured with both methods in 66 samples; correlation of results was unsatisfactory and definitely lower results were obtained with the photometrical procedure. No correlation could be found as well when chymotrypsin activities were measured in stool homogenates on the one hand, and in the supernatant of stools after centrifugation on the other hand, by the titrimetrical or by the photometrical method. Results obtained titrimetrically as well as photometrically after activation of chymotrypsin in pancreatic juice correlated well; the same was true for 2 photometric procedures tested (Imondi, Nagel). Stimulation of the exocrine pancreas with one Lundh meal did not result in any significant increase of fecal chymotrypsin activity in 12 persons tested.

Topics: Buffers; Chymotrypsin; Feces; Humans; Pancreatic Diseases; Pancreatic Juice; Photometry

Topics: Chymotrypsin; Clinical Enzyme Tests; Feces; Humans; Pancreatic Diseases; Trypsin

The function of the exocrine pancreas was examined by the secretin-pancreozymin-test in 3 patients with Wilson's disease. In all cases we found a partial insufficiency. At the time of investigation the patients were 6(7)/12, 11(6)/12 and 21 years old. The youngest one was examined before therapy with D-Penicillamin. We suppose that storage of copper in lysosomes causes a cytotoxic damage of the exocrine part of the pancreas requiring substitution therapy in advanced cases.

Topics: Adult; Ceruloplasmin; Child; Chymotrypsin; Copper; Hepatolenticular Degeneration; Humans; Lysosomes; Male; Pancreas; Pancreatic Diseases; Penicillamine; Trypsin

Chymotrypsin output in the stools (u./24 hr.) has been calculated from analysis of single stool samples, using cuprous isothiocyanate as a continuous marker. The values thus calculated agreed favorably with those calculated from three-day stool collections. In 45 controls, with and without steatorrhea, chymotrypsin output was above 10,000 u./24 hr. In six patients with pancreatic insufficiency the values were considerably lower. In 10 patients with pancreatic disease without insufficiency the values were in the normal range. The method was found very useful in the diagnosis of pancreatic insufficiency. It was not sensitive enough to detect lesser degrees of pancreatic damage.

Topics: Chymotrypsin; Copper; Evaluation Studies as Topic; Feces; Methods; Pancreatic Diseases; Secretory Rate; Specimen Handling; Thiocyanates

Topics: Adult; Aged; Chronic Disease; Chymotrypsin; Feces; Female; Humans; Male; Middle Aged; Neoplasm Metastasis; Pancreatic Diseases; Pancreatic Neoplasms; Pancreatitis

Topics: Child; Chymotrypsin; Clinical Enzyme Tests; Humans; Lipase; Pancreatic Diseases; Trypsin

Topics: Chymotrypsin; Clinical Enzyme Tests; Feces; Humans; Pancreatic Diseases

After a single dose of up to 50 mg/kg body weight (optimal amount for the test) of p-aminobenzoic acid or the corresponding amount of synthetic chymotrypsin substrate N-acetyl-L-tyrosyl-p-aminobenzoic acid, the urinary excretion of p-aminobenzoic acid in rats increases approximately linearly during 24 h. Higher doses do not cause any further significant increase in the amount of urine excreted p-aminobenzoic acid. Compared with a 24 h collecting period, 82% of p-aminobenzoic acid and 77% of p-aminobenzoic acid from N-acetyl-L-tyrosyl-p-aminobenzoic acid were excreted in the urine during the first 6 h after oral application of these substances. Therefore it is sufficient for practical purposes to determine p-aminobenzoic acid in 6 h urine samples. Stimulation of pancreatic secretion by application of 2.5 U of pancreozymin and 2.5 U of secretin failed to bring about significant increase in the cleaved p-aminobenzoic acid in the urine.

Topics: 4-Aminobenzoic Acid; Animals; Chymotrypsin; Clinical Enzyme Tests; Female; Pancreatic Diseases; Peptide Fragments; Rats; Tyrosine

Topics: Aminobenzoates; Animals; Chymotrypsin; Clinical Enzyme Tests; Female; Pancreas; Pancreatic Diseases; Peptides; Rats

A specific substrate (Suphepa), which is well known in duodenal chymotrypsin determination (pancreozymin-secretin-test), is also suitable for the enzyme determination in stools from patients suspected of having a pancreas insufficiency of exocrine nature. The median value of 353 fecal chymotrypsin determination of 180 normal persons was 137 mug/g of native stool. There is a good correlation in comparing the fecal with the duodenal chymotrypsin: Out of 30 comparable patients, 10 patients had pathological values for the duodenal and fecal chymotrypsin determinations, whereas 18 patients had normal values. According to the results of the pancreozymin-secretin-test, false normal stool results were recorded for two patients. No false positive stool values were recorded for the comparative collective. The great accuracy, the modest instrumental expense and the negligible inconvenience for the patient are good in line with the requirements for a screening test.

Topics: Acute Disease; Anilides; Cholecystokinin; Chronic Disease; Chymotrypsin; Diagnosis, Differential; Duodenum; Evaluation Studies as Topic; False Negative Reactions; False Positive Reactions; Feces; Humans; Indicators and Reagents; Intestinal Secretions; Pancreatic Diseases; Phenylalanine; Recurrence; Secretin

Topics: Anilides; Chymotrypsin; Feces; Humans; Methods; Pancreatic Diseases; Phenylalanine

Topics: Cholecystokinin; Chymotrypsin; Duodenum; Endoscopy; Humans; Intubation, Gastrointestinal; Pancreas; Pancreatic Diseases; Pancreatic Juice; Pancreatic Neoplasms; Radiography; Trypsin

Topics: Amylases; Aspergillus; Bile; Bromelains; Chymotrypsin; Enzyme Activation; Enzymes; Humans; Hydrogen-Ion Concentration; Lipase; Pancreas; Pancreatic Diseases; Pancreatic Extracts; Pancreatin; Peptide Hydrolases; Proteins; Stomach; Time Factors; Tissue Extracts; Trypsin

Topics: Aged; Alcoholism; Biopsy, Needle; Cholecystokinin; Chymotrypsin; Drainage; Duodenum; Eating; Fatty Liver; Feces; Female; Humans; Lipid Metabolism; Lipids; Liver; Liver Cirrhosis; Malabsorption Syndromes; Male; Middle Aged; Pancreas; Pancreatic Diseases; Secretin

Topics: Amylases; Cholecystokinin; Chymotrypsin; Clinical Enzyme Tests; Humans; Lipase; Pancreatic Diseases; Trypsin

Topics: Chymotrypsin; False Negative Reactions; Feces; Humans; Pancreatic Diseases

Topics: Amylases; Bicarbonates; Bile Pigments; Blood Glucose; Blood Protein Electrophoresis; Chymotrypsin; Duodenal Diseases; Humans; Lipase; Pancreatic Diseases; Pancreatic Ducts; Pancreatic Juice; Pancreatic Neoplasms; Pancreatitis; Stomach Diseases; Trypsin

Topics: Chymotrypsin; Feces; Humans; Pancreatic Diseases

Topics: Adult; Aged; Chymotrypsin; Clinical Enzyme Tests; False Negative Reactions; False Positive Reactions; Feces; Female; Gastrointestinal Diseases; Humans; Male; Middle Aged; Pancreatectomy; Pancreatic Diseases

Topics: Adolescent; Adult; Amylases; Bicarbonates; Cholecystokinin; Chronic Disease; Chymotrypsin; Clinical Enzyme Tests; Cobalt Radioisotopes; Diabetes Mellitus, Type 1; Female; Humans; Injections, Intravenous; Lipase; Male; Pancreatic Diseases; Pancreatitis; Proteins; Secretin; Trypsin; Vitamin B 12

Topics: Amylases; Chymotrypsin; Enzyme Activation; Humans; In Vitro Techniques; Lipase; Pancreatic Diseases; Pancreatic Extracts; Therapeutic Equivalency; Trypsin

Topics: Amylases; Animals; Choline Deficiency; Chymotrypsin; Lipase; Lipomatosis; Male; Pancreas; Pancreatic Diseases; Penicillamine; Phospholipases; Rats; Trypsin

Topics: Celiac Disease; Cholesterol; Chromium; Chymotrypsin; Expert Testimony; Feces; Follow-Up Studies; Humans; Intestinal Diseases; Lipoproteins; Male; Middle Aged; Occupational Diseases; Pancreas; Pancreatic Diseases; Trypsin

Hog pancreas was subfractionated and assessed for its ability to correct vitamin B(12) malabsorption in patients with pancreatic dysfunction and in rats with partial pancreatic extirpation. The constituent obtained from the pancreas that increased vitamin B(12) absorption in both humans and rats was soluble at 50,000 g, heat labile, acid stable, and approximately 20,000-25,0000 in molecular weight. The active subfractions contained tryptic and chymotryptic but no amylase or lipase activity. Thrice-crystallized trypsin corrected the vitamin B(12) malabsorption in both patients with pancreatic insufficiency and in rats with subtotal pancreatectomy. These data indicate that pancreatic proteolytic enzymes-in particular, trypsin-are necessary for optimal vitamin B(12) absorption.

Topics: Amylases; Animals; Centrifugation; Chromatography, Gel; Chymotrypsin; Cobalt Isotopes; Drug Stability; Lipase; Male; Molecular Weight; Pancreas; Pancreatectomy; Pancreatic Diseases; Rats; Solubility; Swine; Temperature; Tissue Extracts; Trypsin; Ultrafiltration; Vitamin B 12

Topics: Body Weight; Celiac Disease; Child, Preschool; Chymotrypsin; Cystic Fibrosis; Duodenum; Feces; Humans; Infant; Intestinal Diseases; Liver Diseases; Pancreas; Pancreatic Diseases; Time Factors

Topics: Chymotrypsin; Feces; Humans; Lipids; Pancreatic Diseases; Trypsin

Topics: Buffers; Chronic Disease; Chymotrypsin; Clinical Enzyme Tests; Feces; Humans; Indicators and Reagents; Methods; Pancreas; Pancreatic Diseases; Pancreatic Neoplasms; Pancreatitis; Postoperative Complications

Topics: Amylases; Cholecystokinin; Chronic Disease; Chymotrypsin; Clinical Enzyme Tests; Feces; Humans; Lipase; Pancreatic Diseases; Pancreatic Juice; Secretin; Secretory Rate; Stimulation, Chemical; Trypsin

A new approach in the diagnosis of exocrine pancreatic insufficiency has been evaluated in animals. The method involves the oral administration of a chymotrypsin-labile peptide which contains p-aminobenzoic acid (PABA) as a tracer group. In the small bowel in the presence of chymotrypsin, the PABA is split from the peptide and is rapidly absorbed. The amount of PABA (as total aromatic amines) recovered in the urine during the six hours after the dose is used as an index of exocrine pancreatic function. The procedure has been shown to be reliable in detecting surgically induced pancreatic insufficiency in rats, swine, and dogs.

Topics: Administration, Oral; Aminobenzoates; Animals; Chymotrypsin; Dogs; Female; Intestinal Absorption; Intestine, Small; Male; Methods; Pancreas; Pancreatic Diseases; Pancreatin; Peptides; Rats; Swine; Time Factors

Topics: Animals; Chronic Disease; Chymotrypsin; Dog Diseases; Dogs; Malabsorption Syndromes; Pancreas; Pancreatic Diseases; Trypsin

Topics: Autoanalysis; Chymotrypsin; Clinical Laboratory Techniques; Duodenum; Hydrogen-Ion Concentration; Intestinal Secretions; Lipase; Pancreatic Diseases; Photometry; Trypsin

Topics: Cholecystokinin; Chymotrypsin; Duodenum; Humans; Pancreas; Pancreatic Diseases; Pancreatic Neoplasms; Pancreatitis; Secretin; Trypsin

Topics: Acute Disease; Adult; Aged; Bicarbonates; Cholecystokinin; Chronic Disease; Chymotrypsin; Female; Food; Humans; Male; Methods; Middle Aged; Pancreas; Pancreatic Diseases; Pancreatic Juice; Secretin

Topics: Amylases; Bicarbonates; Chymotrypsin; Humans; Lipase; Pancreatic Diseases; Pancreatic Juice; Secretin; Stimulation, Chemical; Trypsin

Topics: Animals; Chymotrypsin; Dietary Fats; Dietary Proteins; Disease Models, Animal; Feces; Female; Intestinal Absorption; Jejunum; Ligation; Lipase; Lipid Metabolism; Lipids; Male; Pancreatic Diseases; Pancreatic Ducts; Pancreatin; Proteins; Swine; Trypsin

Topics: Animals; Chymotrypsin; Clinical Enzyme Tests; Dog Diseases; Dogs; Feces; Female; Gastroenteritis; Male; Pancreatic Diseases; Trypsin

Topics: Amylases; Chymotrypsin; Glycoside Hydrolases; Hormones; Humans; Lipase; Pancreas; Pancreatic Diseases; Pancreatic Juice; Peptide Hydrolases; Trypsin

Trypsin and chymotrypsin concentrations were determined in 180 spot stool specimens from 110 control patients in hospital. The lower limit of normality for each enzyme was placed at the 5% level: 95% of this population excreted feces containing more than 100 mug. of chymotrypsin and 30 mug. of trypsin per g. of feces. Chymotrypsin concentrations appeared to be a more reliable guide to pancreatic function than trypsin concentrations.Fecal chymotrypsin concentrations were subnormal in five patients with chronic pancreatitis, borderline in one patient with relapsing pancreatitis, subnormal in one patient after pancreatectomy, and subnormal in five of nine with carcinoma of the pancreas. Subnormal concentrations of fecal chymotrypsin were found in seven of 21 patients with chronic liver disease related to alcoholism, eight of 32 with a partial gastrectomy, three of 10 with adult celiac disease and five of 16 with psoriasis.It appears that the determination of fecal chymotrypsin concentrations provides a valuable screening test for pancreatic exocrine deficiency. However, normal results may be found in some patients with pancreatic disease and subnormal values may occur in some patients with other conditions.

Topics: Alcoholism; Chymotrypsin; Feces; Humans; Liver Cirrhosis; Malabsorption Syndromes; Pancreatic Diseases; Pancreatic Neoplasms; Pancreatitis; Skin Diseases; Trypsin

Topics: Cholecystokinin; Chymotrypsin; Duodenum; Humans; Methods; Pancreatic Diseases; Secretin; Trypsin

Topics: Acute Disease; Adult; Amylases; Cholecystokinin; Cholesterol; Chylomicrons; Chymotrypsin; Exocrine Glands; Female; Humans; Hyperlipidemias; Lipoproteins; Male; Middle Aged; Pancreas; Pancreatic Diseases; Pancreatitis; Secretin; Triglycerides

Topics: Amino Acids; Animals; Aspartate Aminotransferases; Atrophy; Carbon Isotopes; Chickens; Chymotrypsin; Deficiency Diseases; Diet; Disease Susceptibility; Feces; Glycerides; Intestinal Absorption; Lipase; Lipid Metabolism; Pancreas; Pancreatic Diseases; Selenium; Trypsin; Vitamin E

Topics: Bicarbonates; Chymotrypsin; Feces; Humans; Mathematics; Pancreatic Diseases; Secretin; Temperature; Time Factors

Topics: Amylases; Animals; Cell Membrane; Chymotrypsin; Enzyme Precursors; Hypertrophy; Male; Nucleic Acids; Pancreas; Pancreatic Diseases; Proteins; Rats; Trypsin Inhibitors; Trypsinogen

Topics: Amylases; Carboxypeptidases; Chymotrypsin; Endopeptidases; Esterases; Humans; Lipase; Pancreas; Pancreatic Diseases; Tablets; Trypsin

Topics: Amylases; Chymotrypsin; Cystic Fibrosis; Endomyocardial Fibrosis; Humans; Infant; Infant, Newborn; Lipase; Lipomatosis; Male; Myocardium; Pancreas; Pancreatic Diseases; Pancreatic Juice; Pancreatin; Trypsin

Topics: Acute Disease; Amylases; Chronic Disease; Chymotrypsin; Diagnosis, Differential; Feces; Gastric Juice; Humans; Lipase; Lipids; Pancreatic Diseases; Pancreatic Neoplasms; Pancreatitis; Preoperative Care; Trypsin

Topics: Adult; Aged; Amylases; Biliary Tract Diseases; Bromelains; Chymotrypsin; Clioquinol; Dehydrocholic Acid; Diarrhea; Endopeptidases; Gastric Acidity Determination; Gastrointestinal Agents; Humans; Lipase; Liver Diseases; Middle Aged; Oxyphenonium; Pancreatic Diseases; Pancreatin; Phenanthrolines; Stomach Diseases; Trypsin

Topics: Amylases; Cholecystokinin; Chymotrypsin; Feces; Humans; Pancreatic Diseases; Secretin; Trypsin

Topics: Caproates; Chemical Phenomena; Chemistry; Chymotrypsin; Esters; Fatty Acids; Fluoresceins; Lipase; Palmitic Acids; Pancreatic Diseases

Topics: Amylases; Carboxypeptidases; Cholecystokinin; Chymotrypsin; Duodenum; Electrophoresis; Humans; Isoflurophate; Lipase; Pancreas; Pancreatic Diseases; Secretin; Trypsin

Topics: Adult; Animals; Bile; Chymotrypsin; Dogs; Female; Humans; Male; Microscopy, Electron; Middle Aged; Pancreatic Diseases; Pancreatic Ducts; Pancreatitis; Trypsin

Topics: Chymotrypsin; Fatty Acids; Feces; Humans; Oleic Acids; Pancreatic Diseases

Topics: Amylases; Bicarbonates; Carboxypeptidases; Chymotrypsin; Gastrectomy; Humans; Lipase; Pancreas; Pancreatic Diseases; Pancreatic Juice; Trypsin

Topics: Animals; Chymotrypsin; Ethanol; Glycine max; Growth; Hot Temperature; Hypertrophy; Intestine, Small; Male; Methionine; Pancreatic Diseases; Poultry; Proteins; Rats; Trypsin Inhibitors

Topics: Chymotrypsin; Feces; Humans; Pancreatic Diseases; Trypsin

Topics: Chymotrypsin; Feces; Humans; Infant, Newborn; Intestinal Obstruction; Meconium; Pancreas; Pancreatic Diseases; Trypsin

Topics: Adult; Chymotrypsin; Crohn Disease; Feces; Gastrointestinal Diseases; Humans; In Vitro Techniques; Pancreatic Diseases; Postgastrectomy Syndromes; Trypsin

Topics: Celiac Disease; Chronic Disease; Chymotrypsin; Diagnosis, Differential; Feces; Glucose Tolerance Test; Humans; Internal Medicine; Pancreatic Diseases; Pancreatitis; Radiography

Topics: Amylases; Carboxypeptidases; Chymotrypsin; Duodenum; Emulsions; Glycogen; Humans; Pancreatic Diseases; Peptide Hydrolases; Trypsin

Topics: Black People; Calcinosis; Chymotrypsin; Diagnosis; Feces; Humans; Pancreas; Pancreatic Diseases; Trypsin; Uganda

Topics: Chymotrypsin; Cystic Fibrosis; Disease; Duodenum; Humans; Intestinal Secretions; Pancreas; Pancreatic Diseases; Peptide Hydrolases