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)

The intestinal loop technique was used to evaluate the response of three week old piglets to the heat labile (LT) and the heat stable (ST) enterotoxins produced by Escherichia coli F11(P155). The serum anti-LT activity and the lipase, amylase and trypsin activities in the jejunal lumen of these pigs were determined. Piglets responded independently ti each toxin and no relationship between these responses and serum anti-LT activity or the enzyme activities of the jejunal content could be demonstrated.
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PMID:Relationships of intestinal enzymes and serum antitoxin to the pig response to Escherichia coli enterotoxin. 110 Feb 3

Subcutaneous fat necrosis, a type of panniculitis, is a rare entity that is manifested by painless or painful subcutaneous nodules on the legs, buttocks, or trunk and is associated with pancreatitis or carcinoma of the pancreas, either of which may be asymptomatic. The histopathological findings are pathognomonic and consist of subcutaneous focal fat necrosis and "ghost-like" cells with thick, shadowy walls and no nuclei. Arthritis, particularly of the ankles, is a commonly associated finding. Distant foci of fat necrosis in pancreatic disease are probably due to the local action of hematogenous-borne trypsin and lipase. Since the underlying pancreatic disease may be asymptomatic, histopathologic study of all cases of panniculitis should be considered.
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PMID:Subcutaneous fat necrosis associated with pancreatic disease. 112 53

An in vitro system of guinea pig pancreatic lobules convenient for the study of secretory processes is described in this paper. In this system: (a) the over-all glandular architecture of the tissue is preserved: lobules remain morphologically intact through 5 hours; (b) amylase discharge from unstimulated lobules is low (similar to 4%/hour) and linear over the 5 hours tested; (c) response to carbamylcholine chloride (10-5 M) is energy-dependent, rapid, and extensive (92% discharge of amylase by 5 hours); (d) initial rates of discharge remain stable over the first 3 hours; and (e) no autoactivation of zymogens occurs in incubation medium or tissue. The activation of four zymogens, i.e. chymotrypsinogen, trypsinogen, and procarboxypeptidases A and B, was studied using the following criteria for optimal activation: (a) maximal activation attainable under experimental conditions; (b) stability at the level of maximal activation; and (c) linear relationship between amounts of protein activated and enzyme activity elicited by activation. The concentration of activators (trypsin or enterokinase) and secretory protein, the presence or agents (bovine plasma albumin or Triton X-100) which minimize adsorptive losses of secretory protein on glass or plastic surfaces, and the temperature at which activation is carried out were found to be critical and different for each of the zymogens tested. The kinetics of the appearance of three enzyme activities (amylase, lipase, and ribonuclease) and four potential proteolytic activities (chymotrypsinogen, trypsinogen, and procarboxypeptidases A and B) into the incubation medium was studied under different conditions; i.e. rest and stimulation with various secretogogues (carbamylcholine chloride, caerulein, and pancreozymin). All seven activities estimated to represent similar to 75% of the secretory protein output of the exocrine pancreas were discharged in synchrony and in constant proportions and were released from the tissue to the same extent under each experimental condition investigated.
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PMID:Studies on the guinea pig pancreas. Parallel discharge of exocrine enzyme activities. 112 25

Six fistulated pigs have been used in this experiment to study the effect, on the exocrine pancreatic secretion, of a partial acute irradiation, at 600 rd and 800 rd. Whatever the dose, the irradiation provoked an immediate and temporary decrease of the pancreatic secretion. The normal values were reached after the 8th day post-irradiation. Furthermore, a direct effect on the synthesis of amylase and lipase was shown. The synthesis of trypsin and chymotrypsin was not modified by irradiation.
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PMID:[Effect of acute irradiation on the exocrine secretion of pancreas in pig]. 113 98

Pancreatic function tests were performed in 15 patients with advanced renal insufficiency. Pancreatic secretion was stimulated with CCK/PZ and secretin and 60 minutes later with bile given intraduodenally and CCK/PZ and secretin intravenously. The Wilcoxon-test showed that there were significantly higher lipase levels in serum and lower amylase amounts in duodenal juice compared to normal volunteers. No differences could be demonstratd for volume, maximal bicarbonate concentration, lipase and trypsin outputs. It could be shown by nonlinear discriminant analysis that pancreatic secretion might specifically be changed in patients with chronic renal failure. These patients can be definitely differentiated according to the secretion pattern from normal controls and patients with chronic pancreatitis, pancreatic carcinoma, chronic and acute duodenal ulcer.
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PMID:[Pancreatic secretion of patients with chronic renal insufficiency (author's transl)]. 114 6

1. Intestinal brush border enzymes have heterogeneous rates of turnover, the largest proteins having the fastest turnover. Since the membrane faces the intestinal lumen, the effects of pancreatic factors were examined in mediating this turnover. Surgical subtotal pancreatectomy was used as an experimental model to study the turnover of brush border proteins in the absence of most pancreatic secretions. 2. Subtotal (95%) pancreatectomy of rats was found to cause elevations by about 50% of total activity and specific activities of certain brush border enzymes (maltase, sucrase, lactase), but not of others (alkaline phosphatase, trehalase). Rats were judged to be functionally deficient in pancreatic proteolytic enzymes (a) by demonstration of vitamin B-12 malabsorption, which was corrected by trypsin, and (b) by the finding of only about 20% of proteolytic activity appearing in the lumen after a test meal when compared to control. 3. To measure protein turnover in vivo the method of double labelling was used, where [3H]- and [14C]valine were administered intraduodenally in sequence 10 h apart. With this technique, a high 3H/14C ratio is correlated with rapid turnover. Proteins with apparent molecular weights of about 200 000-270 000 were found to turn over more rapidly than smaller proteins. 3H/14C ranged from 4.7 to 6.2 in animals without pancreatic insufficiency. In the face of decreased pancreatic proteolysis, the 3H/14C ratio was 2.3-3.1, similar to that of proteins with a slow half life. 4. Estimates of relative synthetic rates of large brush border proteins were lower than normal in pancreatectomized animals, but were constant over the period of the labelling experiment. The high enzyme levels in the face of lower synthetic rates confirms that, at the new steady rate, degradation rates must be slower for large brush border proteins in pancreatic insufficiency. 5. In vitro, using purified brush borders, unfractionated pancreatic enzymes were found to remove sucrase, maltase and lactase, but not alkaline phosphatase and trehalase. The enzyme most potent in this respect was the pancreatic protease, elastase. Non-proteolytic enzymes (amylase, lipase, phospholipase A) were inactive in removing enzyme from the brush border. The addition of elastase to pancreatectomized animals in vivo restored the rapid turnover rate of large brush border proteins. 6. A model is thus proposed for the normal catabolism of some large intestinal brush border proteins. It is suggested that the surface of intestinal absorptive cells is being constantly remodelled, and that certain surface enzymes are in part removed from the membrane by the action of pancreatic proteases. A possible special role for elastase is suggested.
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PMID:The possible role of pancreatic proteases in the turnover of intestinal brush border proteins. 114 88

Human milk contains a bile salt-stimulated lipase in amounts that, at pH 6.5 and in the presence of bile salts, might account for a total hydrolysis of the milk triacylglycerols in less than 30 min. In the absence of bile salts the enzyme has no activity against milk fat or against emulsified trioleylglycerol. The primary bile salts sodium cholate and sodium chenodeoxycholate and their taurine and glycine conjugates, but not the secondary bile salt sodium deoxycholate or its taurine and glycine conjugates, caused a pronounced activation of the enzyme against emulsified trioleylglycerol. The lipase was stable at pH 3.5 and 37 degrees C for 1 hour. It was inactivated when incubated with trypsin or chymotrypsin at pH 6.5 but these inactivations were almost abolished in the presence of bile salts. High concentrations of pepsin slowly inactivated the enzyme at pH 4.0. The bile salt-stimulated lipase in human milk is thus stable enough to be active in the intestine, and it is present in high enough activity to contribute significantly to the hydrolysis of the milk triaclyglycerols in the intestine.
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PMID:Human milk lipases. III. Physiological implications of the bile salt-stimulated lipase. 114 84

The trypsin-inhibitory activity observed in cooked soybeans fermented by Rhizopus oligosporus (fungus used in tempeh fermentation) has been examined. The active compounds have now been isolated by ethanol extraction and thin-layer chromatography and have been identified as free fatty acids by infrared spectroscopy and gas-liquid chromatography. Oleic, lineoleic, and linolenic acids are primarily responsible for the increased trypsin-inhibiting activity of cooked soybeans after fermentation. The free fatty acids are liberated from oil in the soybeans by fungal lipase, and they differ from other reported soybean trypsin inhibitors that are protein in nature. Free fatty acids have been previously reported to inhibit various enzymes, such as glycolytic, glyconeogenic, lipogenic, and also proteolytic. Their effect appears to be a nonspecific type of inhibition. Further studies are required to determine their physiological relevance, if any.
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PMID:Free fatty acids identified as antitryptic factor in soybeans fermented by Rhizopus oligosporus. 117 38

Elastolytic activity of human duodenal contents was determined using the new chromogenic substrate succinyl-trialanine-p-nitroanilide (Suc-Ala3-NAp). The mean output values after pancreatic stimulation with pancreozymin and secretin were significantly higher in controls than in subjects with impairment of other secretory values (volume, bicarbonate, amylase, lipase). Agar gel electrophoresis and chromatography on DEAE-Sephadex revealed one to two fractions which differed in mobility (cathodic and anodic fraction), elution with different NaCl concentrations (0.15 M, cathodic fraction; 0.3 M, anodic fraction), and in behaviour towards synthetic and natural substrate (Suc-Ala3-NAp) and elastin-Congo Red). The cathodic fraction cleaved both substrates, whereas the anodic fraction cleaved only Suc-Ala3-NAp. After trypsin and enterokinase treatment the anodic fraction behaved as the cathodic fraction on DEAE-Sephadex chromatography. The molecular weights (Sephadex G-100) and the Michaelis constants (Suc-Ala3-NAp) of both fractions were identical (24 500; 0.45 X 10(-3) M). These fractions represent probably diffenent activation forms of pancreatic elastase.
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PMID:Elastolytic activity of human duodenal contents. 117 3

Sporocysts from the protozoan parasite, Eimeria tenella, were isolated, preincubated with sodium taurocholate, and treated with various preparations of pancreatic enzymes. Crude trypsin, crude lipase, and purified alpha-chymotrypsin all could break the shells of sporocysts and release sporozoites. Purified trypsin was much less active than crude trypsin and purified lipase showed no activity at all. Specific inhibitors of chymotrypsin, tosyl-L-phenylalanyl chloromethane, diphenylcarbamyl chloride, and chymostatin inhibited the release of sporozoites by all the enzyme samples, whereas tosyl-L-lysyl chloromethane, a specific inhibitor of trypsin, exerted no inhibitory effect. It is thus postulated that chymotrypsin, not trypsin, is an essential enzyme involved in excystation of E. tenella. Purified chymotrypsin is recommended to replace crude trypsin in the vitro excystation of E. tenella as a likely improved procedure.
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PMID:Pancreatic chymotrypsin as the essential enzyme for excystation of Eimeria tenella. 118 37


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