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)

We differentiate indirect and direct methods. The indirect methods include the examination of the blood (ESR, blood picture, electrolytes, especially calcium, for the exclusion of hyperparathyroidism, status of fat and liver enzymes, activity of alpha-amylase and lipase. More informative than a serum determination is the measurement of the amylase activity in the 24-hour urine. The detection of chymotrypsin in the stool can be recommended as an investigative test also for use in general practive in collaboration with a central laboratory.- The direct methods include investigation of the duodenal juice with measurement of pH, bicarbonate, of the activities of chymotrypsin, trypsin, lipase and amylase. For excluding of a disturbance of the carbohydrate metabolism in addition to blood sugar determinations, glucose tolerance and tolbutamide tests, the determination of insulin activity is indicated.
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PMID:[Chemical Investigation of Chronic Pancreatitis]. 0 30

The activity of amylase, sucrase, protease and lipase has been examined in Wallago attu, Clarias batrachus and Labeo rohita. The optimum pH value for carbohydrases ranges from 5.0 to 7.0 and that for trypsin between pH 6.8 and 7.8. Lipase is active at a slightly more alkaline medium. The optimum pH for a given enzyme varies in different sections of the alimentary canal of the same fish and also from species to species. Variations are also found in the optimum substrate concentration for a given enzyme in the different sections of the alimentary canal. The activity of carbohydrases is higher in the herbivorous fish Labeo, than in the carnivorous fish Wallago, and the omnivorous fish Clarias. As for protease, maximum activity is found in Wallago. The difference is not so well marked for the activity of lipase. There is a correlation between the normal diet of the fishes and the relative activity of the digestive enzymes.
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PMID:Digestive enzymes of three teleost fishes. 1 77

1. Amylase (EC 3.2.1.1) activity found in the intestinal tract of chicks posterior to the stomach is of endogenous origin, as amylase in the food is inactivated by the low pH in the stomachs. 2. Ingestion of raw soya-bean diet (RSD) or of heated soya-bean diet (HSD) supplemented with trypsin inhibitors induced higher amylase activites in the lower part of the small intestine and caecum as compared with HSD. 3. Ingestion of RSD after ligation at the end of the duodenum, end of the ileum or one of the cacea, or injection of soya-bean trypsin inhibitor into a aligated caecum, indicated that there is no amylase synthesis by the intestinal tract cells or microflora as a response to the presence of RSD or trypsin inhibitors. 4. It seems that amylase found in the digestive tract of the chick is of pancreatic origin and the RSD or trypsin inhibitors induce higher pancreatic amylase secretion than HSD which (the additiona amylase) accumulates mainly in the caeca.
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PMID:The level and origin of amylase (EC 3.2.1.1) in the digestive tract of chicks receiving trypsin inhibitors in their diet. 2 57

Mycobacterium ulcerans produces an exotoxin in culture which, when inoculated into guinea pig skin, causes inflammation, necrosis, edema, and other histopathological changes resembling those in infections of humans. The toxin was resistant to heat and to alkalies and was moderately acid labile. Toxic activity was destroyed by Pronase, phospholipase, lipase, amylase, and glucosidase but not by trypsin, collagenase, cellulase, lysozyme, hyaluronidase, or neuraminidase. Toxic activity was resistant to treatment with 2-mercaptoethanol, urea, guanidine hydrochloride, p-chloromercuribenzoate, ethylenediaminetetraacetate, and sodium deoxycholate but was destroyed by sodium m-periodate and sodium dodecyl sulfate. The toxin was precipitated by a wide range of ammonium sulfate concentrations. Extraction with chlorofrom-methanol or petroleum ether destroyed its activity. Isopycnic density gradient ultracentrifugation in KBr produced a high-density lipoprotein layer with a 24-fold increase in specific activity. The results indicate that this toxin is a high-molecular-weight phospholipoprotein-polysaccharide complex.
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PMID:Further characterization of Mycobacterium ulcerans toxin. 3 Jun 94

The biliary and pancreatic secretions have been determined in patients given pelvic or para-aortic irradiation, with a dose of 50 Gy in the former group and between 36 and 40 Gy in the latter. A test meal containing polyethylene glycol (PEG) as reference substance was used. Each sample of the duodenal content was assayed for volume, PEG content, amylase and trypsin activity, pH and biliary secretion. No significant modifications of biliary and pancreatic secretions were demonstrated after irradiation, suggesting that these functions are not involved in the pathogenesis of the malabsorption radiation syndrome.
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PMID:Biliary and pancreatic secretions in abdominal irradiation. 4 Mar 99

Amphipathic enzymes, invertase (EC 3.2.1.26), 8-amylase (EC 3.2.1.3), and alkaline phosphatase (EC 3.1.3.1), were purified from the rat small intestinal mucosa as trypsin and Triton forms, the catalytic and regulatory characteristics of which were compared in rats and in drosophila. Differences in the catalytic propertiis of the two enzyme forms were demonstrated, which suggested that the hydrophobic part of the enzyme was involved in maintaining optimal conformation of the catalytic part. Many modifiers have beenfound to influence the Triton rather than the trypsin form of the enzyme. It is therefore suggested that the hydrophobic sub-units of the enzymes might be involved in transmitting information from the cytoplasm into the external surface of the membrane, the cell in this way regulating the activity of surface enzymes. If this is indeed the case, it is suggested that the hydrophobic part performs functions not only of external but also of internal regulation.
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PMID:Catalytic and regulatory properties of the Triton and trypsin forms of the brush border hydrolases. 4 Aug 47

Pigs were surgically prepared with external pancreatic fistulae and duodenal cannulae in order to elucidate whether the proposed intestinal feedback control of pancreatic secretion in the pig--as in rat and man--is exerted by trypsin. Furthermore, the effect of intraluminal amylase on pancreatic secretion was studied. Reintroduction of pancreatic juice into the duodenum or infusion of trypsin into the duodenum depressed the volume of the pancreatic flow and the protein output markedly. Introduction of amylase into the duodenum did not significantly affect the pancreatic secretion. Thus, it seemed as it trypsin but not amylase was involved in the suppression exerted by pancreatic juice on exocrine pancreatic secretion in the pig.
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PMID:Effects of intestinal amylase and trypsin on pancreatic secretion in the pig. 9 74

The effect of intraduodenally administered trypsin on pancreatic exocrine secretion was investigated in conscious rats surgically prepared with bile--pancreatic fistulae. Introduction of NaHCO3 into the duodenum did not influence pancreatic secretion. Reintroduction of bile--pancreatic juice into the duodenum, however, suppressed pancreatic protein output, mainly because of changes in protein concentration. Infusion of trypsin into the duodenum in the absence of intraluminal pancreatic juice significantly suppressed the secretory volume and pancreatic enzyme output; addition of trypsin inhibitor to the trypsin infusion resulted in an immediate increase of pancreatic secretion. Trypsin inhibitor per se, however, was without effect. Bile--pancreatic juice affected amylase, kipase, and trypsinogen output in a parallel fashion; after addition of trypsin inhibitor to the infusion the inhibitory effects on pancreatic enzyme output was reversed in a parallel manner. The results support the hypothesis that pancreatic exocrine secretion is regulated by a feedback mechanism exerted--at least partly--by intraluminal trypsin.
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PMID:Trypsin as a regulator of pancreatic secretion in the rat. 9 75

The concentration in serum of cathodal trypsinogen has been studied in certain clinical and experimental situations. The concentration correlated with pancreatic amylase activity. Low levels were found in patients with malabsorption due to exocrine pancreatic insufficiency. The concentration rose after endoscopic retrograde cholangiopancreatographic examinations (ERCP). After ERCP, however, no trypsin was detected complexed with protease inhibitors, as is generally found in acute pancreatitis. The trypsinogen concentration in serum also rose in renal failure indicating a renal elimination route for the endogenous trypsinogen.
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PMID:Studies on the turnover of endogenous cathodal trypsinogen in man. 10 10

In patients without pancreatic disease Aminofusin L forte infused for 1 h did not stimulate gastric or pancreatic secretion. On the other hand, infusion of casein by hydrolysate led to a significant increase in the concentration and total output of HCl. 4 h intravenous infusion of Aminofusin L forte caused a transient but significant rise of the bicarbonate concentration, amylase activity and above all trypsin activity and output. The results show that N solutions used for parenteral protein nutrition influence in a different way both gastric and pancreatic secretion.
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PMID:The effect of some N solutions for parenteral nutrition on gastric and pancreatic secretion. 11 12


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