Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The properties of rat liver cytoplasmic alpha-tocopherol binding protein have been studied. 2. The binding protein sedimented in the 3 S region of sucrose density gradients, and gel filtration indicated an approximate molecular weight of 30 500. 3. Of the tissues examined by the present assay, binding was detectable only in the liver. 4. Optimal binding was achieved by incubation at 26 degrees C for 4 h and was independent of pH between 7.4 and 9.0. 5. Pronase completely abolished binding. The binding protein was, however, almost completely resistant to trypsin, and unaffected by RNAase, DNAase, triacylglycerol lipase, and phospholipase C. 6. A variety of tocopherol analogues and other lipid-soluble compounds were tested for their ability to compete for binding. Only alpha-tocopherol and to a lesser extent alpha-tocotrienol and gamma-tocopherol exhibited competition. alpha-Tocopherol acetate, alpha-tocopherol quinone and 6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid had no effect on binding. 7. Tocopherol binding was reversible, and the tocopherol was not metabolized during incubation.
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PMID:Rat liver alpha-tocopherol binding protein. 87 71

Extensive metabolic studies were conducted in five normal controls and in five study patients after total gastric resection with Roux-en-Y (RY) reconstruction to determine the nutritional consequences of this particular technique of restoring gastrointestinal continuity. Although malabsorption of fat (19.2 +/- 2.2%) and nitrogen (22 +/- 2.5%) demonstrated in the study patients was moderate, it was significantly greater than normal ( less than 0.01). In spite of the demonstrated malabsorption, however, positive nitrogen balances (+ 0.33 +/- 0.18 gm/day) were maintained in the RY patients throughout the investigative period. These observations suggest that malabsorption after RY is infrequently of clinical significance, even in this "worst-case" situation characterized by complete removal of gastric tissue. Malnutrition should occur in only those patients with more limited gastric resections and RY reconstruction who are unable to increase caloric intake to cover losses due to malabsorption. A significant decrease in both trypsin and lipase concentrations and a marked delay in secretion of these enzymes was noted in the RY patients in response to a test meal (p less than 0.01). Malabsorption of fat and nitrogen in RY patients improved after exogenous pancreatic enzymes, but not after administration of tetracycline. Bacterial overgrowth as a cause of postoperative malabsorption may be less important than previously thought. Malabsorption after RY is due primarily to maldigestion brought about by duodenal bypass which, in turn, results in either an absolute or a relative pancreatic enzyme insufficiency.
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PMID:Pathophysiology and significance of malabsorption after Roux-en-Y reconstruction. 87 Oct 13

The action of pancreatic amylase, trypsin, lipase, and whole pancreatin was tested on five strains of Bibrio cholerae. Amylase did not act on any strain in concentrations to 10,000 IU/ml whereas trypsin increased vacuolization and lipase enhanced retraction of the protoplasm particularly in 2 of the 5 tested vibrio strains. Pancreatin caused damage hoth of the cell wall and the cytoplasm. It is suggested that these enzymes may play a role in the defense of the body against cholera vibrios.
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PMID:Action of some pancreatic enzymes on Vibrio cholerae. 87 87

We undertook to test the recent suggestion that measurement of immunoreactive carcinoembryonic antigen (CEA) in pancreatic secretion may be useful in diagnosis of pancreatic cancer. Using duodenal intubation and a perfusion method in 57 cases, we measured the rate of pancreatic CEA secretion into the duodenum under basal saline perfusion, alone and with continuous intravenous infusion of secretin (2 clinical units per kg per hr) and of cholecystokinin-pancreozymin (CCK, 15 Crick-Harper-Raper units per kg per hr); and we compared the CEA output with secretion of trypsin, lipase, and bicarbonate under the same conditions. Subsequent laparotomy revealed pancreatic carcinoma in 25 patients, pancreatitis in 7, other intraabdominal malignancies in 6, and benign nonpancreatic disorders in 19. CEA output rates did not differentiate all pancreatic-cancer patients from other patients in any test condition. However, pancreatic enzyme outputs were abnormal with almost 90% of cancers of the pancreatic head and with 75% of cancers of the pancreatic body and tail. For detection of pancreatic cancer, enzyme and bicarbonate outputs in response to CCK are more accurate than pancreatic CEA or bicarbonate outputs in response to secretin. Since CCK-stimulated enzyme outputs can be related accurately to malabsorption (not reported here), we prefer them to bicarbonate output for assessment of pancreatic function.
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PMID:Prospective evaluation of the pancreatic secretion of immunoreactive carcinoembryonic antigen, enzyme, and bicarbonate in patients suspected of having pancreatic cancer. 89 42

A strain of Actinomyces odontolyticus, originally isolated from human dental plaque, produced a non-dialyzable, trypsin-sensitive substance that was bactericidal for certain strains of bifidobacteria at 42 degrees C but not at 37 degrees C. Detectable quantities of the bacteriocin were not produced in liquid media. Experimentally useful yields were obtained by extraction from pour plate cultures of producer cells. At 42 degrees C, exponential killing did not occur until indicator cells had doubled at least once. At 37 degrees C, the bacteriocin effected a transient bacteriostasis. Partially purified concentrates were obtained by diethylaminoethyl-cellulose chromatography, and such material was not inactivated by ribonuclease, deoxyribonuclease, or lipase. Pronase, trypsin, and exposure to 100 degrees C for 20 min completely abolished activity. Inhibitory activity was considerably reduced by exposure to a pH of either 3 or 11. Treatment of producer cells with curing agents did not induce a high frequency of non-bacteriocinogenic cells. The odontolyticin was adsorbed by susceptible, as well as resistant, bacteria.
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PMID:Bacteriocin from Actinomyces odontolyticus with temperature-dependent killing properties. 90 31

The concentration of trypsin, pancreatic iso-amylase, phospholipase, and lipase were determined in intestinal content during the first two hours of digestion of a test meal. In normal subjects the concentration curves for all enzymes displayed a typical biphasic pattern. In patients with chronic pancreatic disease, the typical variations of the enzyme concentrations were markedly diminished. In patients with celiac disease, the initial peak of the trypsin and phospholipase activities seemed to be delayed, and in patients operated upon with a Polya gastric resection the concentrations of trypsin and phospholipase increased gradually. In these two disorders the lipase concentration curve was of quite a different, uncharacteristic pattern. It is suggested that the concentration curves of the enzymes reflect pancreatic secretion. Furthermore, the secretion of lipase in celiac disease and following gastric resection seems to be 'non-parallel'. Owing to a fairly considerable variation in the values from different individuals, it seems reasonable to conclude that in clinical practice determination of enzyme concentration curves after a test meal probably does not improve the reliability of the conventional Lundh test.
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PMID:Time-related enzyme concentrations in duodenal aspirates after ingestion of a test meal. 91 58

After indirect stimulation of the pancreas by means of a test meal the intestinal activities of trypsin were determined in 452 subjects, lipase in 117, and phospholipase in 57. Trypsin levels were subnormal in 88%, lipase levels in 80%, and phospholipase levels in 81% of patients with chronic pancreatic disease. The outcome of repeated tests (trypsin) was completely consistent in 20 out of 22 patients. Calculations of ratios between the enzymes studied suggested that lipase was the enzyme most susceptible to pancreatic damage. Also in cases of celiac disease and after Polya gastric resection, the decrease of the intestinal lipase concentrations was more marked than that of the other enzymes. In 9% of the cases of chronic pancreatic insufficiency the diagnosis would have been overlooked if either lipase or trypsin had been determined as the sole enzyme. In clinical practice it is recommended to estimate at least two enzymes, because abnormal ratios may be of diagnostic value and because the two different groups of enzymes provide a mutual check on the secretory capacity of pancreatic enzymes. On the whole, the test was found to be reliable, simple, physiological, and inexpensive in terms of resources, and it is highly recommended as a routine test of the pancreatic function.
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PMID:Intestinal activities of trypsin, lipase, and phospholipase after a test meal. An evaluation of 474 examinations. 92 5

The effect of CDCA feeding on pancreatic and intestinal enzymes was studied. Mice were fed 0.5% w/w chenodeoxycholic acid in a normal diet. Pancreatic lipase concentration was significantly increased after 3 days on the CDCA diet, while amylase and trypsin concentrations were significantly higher at 23 days when compared with the controls. At 70 days there was a significant increase in the concentrations of amylase, trypsin, and lipase. Protein concentrations paralleled the rise in enzyme levels. Amylase and lipase, when measured as specific activities, were still higher than the controls at 70 days. Intestinal amylase levels did not change during the experiments, but intestinal alpha-glucosidase activity increased significantly in the CDCA-treated animals. The results are discussed in terms of their similarity with those reported to occur after feeding soybean trypsin inhibitor.
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PMID:Changes in pancreatic and intestinal enzyme activities following chenodeoxycholic acid feeding. 92 7

Under conditions of stimulation with pancreozymine (in doses of 1.5 and 0.5 Units/kg), a specific stimulant of the enzyme secretion of the pancreas, there occurred a significant fall of the concentration and of the amount of lipase and trypsin in the duodenal contents of patients suffering from diabetes mellitus for over 5 years (20 investigations) in comparison with the indices in 14 healthy persons. No disturbances of amylase secretion were found in diabetes. Proceeding from the evidence on the role played by calcium and cyclic 3'--5'-adenosinmonophosphate in the regulation of the external pancreatic secretion the effect of calcium gluconate and euphylline was tested; they appeared to be effective stimulants of pancreatic secretion of the enzymes in patients with diabetes mellitus.
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PMID:[Use of pancreozymin for detection of pancreatic enzyme-secreting insufficiency in diabetic patients and selection of methods of treatment]. 93 82

The interrelationship of enterokinase and trypsin activities were investigated in 133 infants and children with a variety of gastrointestinal and pancreatic disorders. Fourteen patients with diarrhea and grade II mucosal injury revealed a significant (P less than 0.01) reduction of enterokinase, trypsin, and disaccharidase activites as compared to 59 children with normal mucosa. Nine patients with cystic fibrosis and pancreatic insufficiency had normal mucosal enterokinase activity and elevated intraluminal enterokinase activity with very low or no trypsin activity. Patients with hypoproteinemia and gastrointestinal protein loss, associated with intestinal lymphangiectasia (4 patients) and intestinal lymphoid nodular hyperplasia (3 patients), had normal or insignificant decrease of enterokinase and trypsin activities. In patients with steatorrhea, a normal sweat test, normal intestinal mucosa, and absent trypsin activity, two entities were defined. One group (3 patients) was diagnosed as Schwachman-Diamond syndrome with pancreatic insufficiency and normal mucosal and intraluminal enterokinase activity. The second group (2 patients) with absent mucosal and intraluminal enterokinase activity and normal lipase and amylase activities was diagnosed as congenital enterokinase deficiency.
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PMID:Enterokinase and trypsin activities in pancreatic insufficiency and diseases of the small intestine. 94 55


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