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)

Examination of the peritoneal exudates of 12 patients with acute pancreatitis revealed high activities of pancreatic lipase and amylase. The immunologic levels of the plasma-derived inhibitors alpha 1-antitrypsin, antithrombin III and alpha 2-macroglobulin in the peritoneal exudates were not markedly different from those of the plasma. However, the inhibitory capacity of alpha 2-macroglobulin, the main inhibitor of human pancreatic trypsin in the exudate, was almost completely depleted when measured by an enzymatic method. Furthermore, spontaneous fibrinolysis occurred in 6 out of 13 exudates applied to plasminogen-free fibrin plates, indicating the presence of free proteinase. This fibrinolytic activity might be inhibited by exogenous alpha 2-macroglobulin or aprotinin (Trasylol, Bayer AG).
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PMID:Proteinases and inhibitors in plasma and peritoneal exudate in acute pancreatitis. 608 67

The effects of dietary pectin and fat level on digestive enzyme activities in the pancreas and small intestine and on intestinal bile acid levels were investigated. In unfed rats, dietary pectin did not influence the pancreatic enzymes studied, but a higher level of corn oil in the diet lowered the amylase activity in the pancreas, increased pancreatic lipase activity and slightly lowered the chymotrypsin and trypsin activities. Diet did not change the dry weight of the pancreas. In the fed rats, dietary pectin increased the dry weight of the small gut wash plus the mucosal scraping. Dietary pectin increased the small intestinal lipase and chymotrypsin levels and at the low level of fat only, increased amylase and trypsin activities in the small intestine of fed rats. Intestinal lipase levels were higher and amylase levels lower in rats consuming the high level of corn oil. These results indicate that changes in dietary fat level led to changes in the amylase and lipase content of secreted pancreatic juice and that differences in absorption associated with diets containing pectin could be the result of increased material in the small intestine.
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PMID:Effects of dietary pectin and fat on the small intestinal contents and exocrine pancreas of rats. 615 61

In chronic experiments on dogs with fistulae of pancreas, administration of pancreozymin into the cerebral ventricles activated the lipase activity of pancreatic juice whereas secretin inhibited the trypsin activity. The pancreozymin administration into the anterior hypothalamus activated the pancreatic lipase whereas administration of this hormone into the RF exerts no effect on the basal secretion of juice and enzymes. The secretin administration into the hypothalamus or RF leaves the pancreatic secretion intact. Administration of CSF from dogs-donors with pancreozymin in their cisterna magna activated the lipase activity of the juice. Central action of cholecystokinin-pancreozymin on the pancreatic secretion of enzymes seems to be actualized through the hypothalamic structures.
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PMID:[Central action of cholecystokinin-pancreozymin and secretin on pancreatic enzyme secretion]. 617 May 32

The activities of pancreatic lipase, pancreatic amylase, and trypsin were followed after storage at -20 degrees C in duodenal juices collected after pancreatic stimulation by either a test meal or exogenous hormones. The activities of all three enzymes were stable for up to one year in juices collected after a test meal. However, in nine out of 10 hormonally stimulated juices, lipase activities fell to less than 50% of the initial activity within three weeks of storage, and in a third, trypsin activities fell to less than 60% over a similar period. Amylase activity remained relatively unchanged. The in-vitro addition of the test meal, its separate components, or glycerol (50%, V/V) stabilised lipase and trypsin activities in hormonally stimulated juices stored at -20 degrees C for at least one month.
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PMID:Stability of pancreatic enzyme activities in duodenal juice after pancreatic stimulation by a test meal or exogenous hormones. 617 75

Purpura was grossly observable in albino mice 6 to 8 h after the intraperitoneal injection of sterile, deoxyribonuclease-treated, cell-free extracts prepared by sodium deoxycholate-induced lysis, sonic disruption, Parr bomb treatment, autolysis without sodium deoxycholate, or alternate freezing and thawing of washed suspensions of Streptococcus pneumoniae type I. Cell-free extracts obtained from sonically disrupted, heat-killed cells (100 degrees C for 20 min) did not contain purpurogenic activity. The reaction was maximal at approximately 24 h postinjection, started to fade slowly after 24 to 48 h, and usually was not grossly observable by 4 to 6 days postinjection. The purpura-producing principle (PPP) in the cell-free extract was purified by sequential ammonium sulfate precipitation, protamine sulfate precipitation, Sepharose 6B gel filtration, wheat germ lectin-Sepharose 6MB affinity chromatography, ribonuclease and trypsin treatment, and a second Sepharose 6B gel filtration step. The final preparation (i) contained glucosamine (5.6%), muramic acid (8.0%), neutral carbohydrate (12.8%), phosphate (8.0%), orcinol-reactive material (6.0%), and Lowry-reactive material (1.6%), and (ii) was free of detectable amounts of deoxyribonucleic acid, capsular polysaccharide, neuraminidase, cytolysin, and hyaluronidase. The isoelectric point and molecular size of the PPP were approximately pI 3.0 and several million daltons, respectively, and the activity remained in the supernatant fluid after centrifugation for 1 day at 105,000 x g. PPP activity was destroyed by incubation with egg white lysozyme and sodium metaperiodate but was resistant to trypsin, pronase, alpha-amylase, deoxyribonuclease, ribonuclease, alkaline phosphatase, pancreatic lipase, 7% trichloroacetic acid, 6 M urea, autoclaving (121 degrees C) for 30 min, and mild acid and alkali exposure. Our observations indicate that the PPP requires intact beta-1,4-glucosidic linkages for activity and support the working hypothesis that activity is associated with pneumococcal peptidoglycan solubilized by the bacterium's autolysin.
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PMID:Characterization of pneumococcal purpura-producing principle. 624 53

Serum samples obtained from 20 insulin-dependent diabetics (IDD), 23 non-insulin-dependent diabetics (NIDD) and 30 controls were assayed for their pancreatic lipase activity, immunoreactive trypsin concentration and glycosylated haemoglobin (HbA1) respectively. The distribution of serum pancreatic lipase activity in normal subjects and diabetics was nonparametric. The median serum lipase activity in IDDs (86 U/l) was significantly lower that that in controls (131 U/l, p less than 0.002) and NIDDs (126 U/l, p less than 0.001). There was a significant correlation between serum pancreatic lipase activity and serum IRT concentration (r = 0.65, p less than 0.001). Neither pancreatic lipase activity nor IRT was related to HbA1 concentrations. These data show for the first time that serum pancreatic lipase activity is diminished in IDDs.
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PMID:Low pancreatic lipase in insulin-dependent diabetics. 633 49

A bacteriocin produced by Bacteroides fragilis 1356 was purified from culture medium and characterized. The spectrum of the inhibitory activity of this bacteriocin was species specific. The bacteriocin was recovered from the initial stages of purification as a complex, greater than 2 X 10(7) daltons in mass, containing protein, lipid, and carbohydrate. The dissociation of this complex by 6.0 M guanidine hydrochloride permitted further purification of the bacteriocin by removal of lipid and carbohydrate. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that the purified bacteriocin was homogeneous, with a relative molecular weight of 5,000. The activity of the purified bacteriocin was not affected by RNase, DNase, phospholipase A, pancreatic lipase, or dextranase, but was destroyed by trypsin, proteinase K, heat (80 degrees C, 30 min), or a pH below 5 or above 8. Amino acid analysis indicated a predominance of acidic and polar amino acids.
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PMID:Purification and characterization of a bacteriocin from Bacteroides fragilis. 635 Feb 64

Patients with cystic fibrosis have been found to have abnormal serum concentrations of immunoreactive trypsin and abnormal activities of pancreatic isoamylase. A study was undertaken to discover whether activity of pancreatic lipase is also altered in cystic fibrosis. Serum from 23 patients with cystic fibrosis was assayed for immunoreactive trypsin and pancreatic lipase. Median serum pancreatic lipase activity was significantly lower in patients with cystic fibrosis than in controls, as was immunoreactive trypsin concentration (p less than 0.0001). Some patients had supranormal lipase concentrations but these were not always associated with absence of malabsorption. Serum pancreatic lipase activity is considerably changed in cystic fibrosis.
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PMID:Serum pancreatic lipase activity in cystic fibrosis. 640 37

Hepatic triglyceride lipase was obtained from post-heparin plasma of rats in an electrophoretically homogeneous form. The enzyme had an isoelectric point at pH 4.9 and molecular weight of 65,000. The relation between the "lipase" and "esterase" activities of the enzyme was studied using emulsified triolein and water-soluble methyl butyrate (80 mM) as substrates. The same enzyme protein catalyzed the hydrolyses of both emulsified triolein and water-soluble methyl butyrate. The relation of activity to the methyl butyrate concentration differed from those for pancreatic lipase and liver esterase. During purification, the ratio of methyl butyrate to triolein-hydrolyzing activity of the enzyme increased. On digestion of the enzyme with trypsin, the "lipase" activity was retained. However, the trypsin-treated enzyme was adsorbed to a heparin-Sepharose column and eluted with 0.75 M NaCl, like the untreated enzyme. These results suggest that rat hepatic triglyceride lipase contains a so-called "hydrophobic recognition site" that is destroyed by trypsin treatment and is distinct from the heparin-binding and catalytic sites.
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PMID:Methyl butyrate-hydrolyzing activity of hepatic triglyceride lipase from rat post-heparin plasma. 646 99

Immunoreactive trypsin (IRT) and pancreatic lipase were measured in serum from 37 geriatric in-patients (median age 77.5 years) without history of diarrhoea, pancreatic disease, diabetes or acute or chronic alcoholic intake. IRT and pancreatic lipase concentrations/activity were strongly correlated and were markedly elevated when compared with a control population of 22 subjects (median age 27 years). Such elevations in pancreatic enzymes indicate a subclinical damage of exocrine pancreatic tissue. Assessment of exocrine pancreatic function in the geriatric age group should not be based on pancreatic enzyme levels in serum.
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PMID:Serum pancreatic enzymes in the elderly. 671 39


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