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)

Assuming that acidic degradation of lipase was the major cause of failure for the correction of steatorrhea by pancreatic extracts, we compared the in vitro and in vivo activities of a fungal lipase (FL) (Rhizopus arrhizus) with classical porcine pancreatic extract (Eurobiol). The choice of FL was determined by its two optimum pH (3.5 and 7.4). Five factors known to modify lipase activity were tested: pH, biliary acids colipase, trypsin and albumin. Bioavailability was measured by using a double intubation method in 13 patients with severe pancreatic insufficiency. Each enzymatic preparation was given during a test meal in a randomized and cross-over fashion. Results of the in vitro study showed that FL differed from pancreatic lipase by the following properties: better resistance in acidic solution, inhibition by biliary salts, absence of effect of colipase and rapid degradation by trypsin. In vivo the percentage of lipase activity recovered was 14.2 +/- 10.6 p. 100 for FL and 56 +/- 50 p. 100 for the classical pancreatic preparation. Compared with placebo significant differences in the recovery rate of lipolytic activity were observed with the pancreatic preparation only and started at the 40th min after the end of the test meal. These results showed that lack of degradation in acidic milieu is not the only valuable criterion for the choice of an efficient lipase preparation. The role of other potential factors such as gastric emptying as well as proteolytic degradation of the enzyme should be considered as well.
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PMID:[Comparison of fungal lipase and pancreatic lipase in exocrine pancreatic insufficiency in man. Study of their in vitro properties and intraduodenal bioavailability]. 322 Feb 31

We compared serum concentrations of cathodic trypsin-like immunoreactivity, pancreatic lipase, and pancreatic isoamylase as diagnostic tests of chronic pancreatitis (and of pancreatic steatorrhea in the 41 patients with steatorrhea) in 105 patients (57 men, 48 women) consecutively investigated because of clinical suspicion of chronic pancreatitis. Chronic pancreatitis (36 patients), pancreatic steatorrhea (24 patients), and other diseases were diagnosed without knowledge of the serum levels of the three enzymes. When evaluated by means of receiver operating characteristic curves, no differences were found in diagnostic performance of the enzymes with regard to chronic pancreatitis or pancreatic steatorrhea. The sensitivity and specificity for recognition of chronic pancreatitis ranged from 0.306 to 0.444 and from 0.942 to 0.986 when the discrimination values were chosen to give highest efficiencies. The similar ranges for pancreatic steatorrhea were 0.500-0.708 and 0.882-0.941. In conclusion, none of the three enzymes had any advantage over the others as diagnostic tests of chronic pancreatitis or of pancreatic steatorrhea. Only positive test results have clinical importance because of the low sensitivities of the three enzymes.
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PMID:Serum cathodic trypsin-like immunoreactivity, pancreatic lipase, and pancreatic isoamylase as diagnostic tests of chronic pancreatitis or pancreatic steatorrhea. 329 Oct 84

Serum elastase 1 was determined in the serum of 38 patients with acute pancreatitis, using specific radioimmunoassay technique. Serving as controls were 36 healthy people, 33 patients with chronic pancreatitis, 49 patients with various GI-tract diseases, and 6 patients with pancreatic carcinoma. Sensitivity of elastase 1 for the diagnosis "acute pancreatitis" was 97% after admission to the hospital and 100% within 48 h after onset of acute pancreatitis. The determination of elastase 1 is clearly superior to that of trypsin, pancreatic lipase, or pancreatic amylase, if diagnosis has to be made more than 48 h after the onset of the disease. The specificity is restricted, because there are some cases with chronic pancreatitis and GI-diseases with raised values. There is no possibility to estimate the severity of acute pancreatitis by measuring serum elastase 1.
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PMID:Diagnostic and prognostic value of serum elastase 1 in acute pancreatitis. 364 49

Lipstatin, a new and very potent inhibitor of pancreatic lipase (the key enzyme of intestinal fat digestion) was isolated from Streptomyces toxytricini. Lipstatin contains a beta-lactone structure that probably accounts for the irreversible lipase inhibition. The IC50 of lipstatin for pancreatic lipase is 0.14 microM. In mice triolein absorption was dose-dependently inhibited by lipstatin, whereas oleic acid was absorbed normally. Other pancreatic enzymes, such as phospholipase A2 and trypsin, were not inhibited even at an inhibitor concentration of 200 microM.
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PMID:Lipstatin, an inhibitor of pancreatic lipase, produced by Streptomyces toxytricini. I. Producing organism, fermentation, isolation and biological activity. 368 18

In 849 patients (417 men, 432 women) consecutively hospitalized with acute abdominal pain we compared the value of serum cathodic trypsin-like immunoreactivity, pancreatic lipase (EC 3.2.1.3) and pancreatic isoamylase (EC 3.2.1.1) as diagnostic tests for acute pancreatitis. The diagnoses of acute pancreatitis (in 49 patients, 5.8%) and other diseases were made without knowledge of these enzyme values. When evaluated by means of receiver operating characteristic curves no differences were found in diagnostic performance of the three enzymes. Use of combinations of different enzymes had no advantage over single enzyme determination using discrimination analysis for evaluation. The highest efficiency was for all three enzymes 0.991 (95% confidence limits: 0.983-0.995) and for all three enzymes the discrimination value giving this efficiency was several times the upper limit of reference range: 1 779 micrograms/l for cathodic trypsin-like immunoreactivity, 831 U/l for pancreatic isoamylase and 316 micrograms/l for pancreatic lipase. None of the enzymes had any prognostic value at admission in predicting a mild or severe attack of acute pancreatitis. In conclusion, no single enzyme or combination of enzymes had any diagnostic advantage for acute pancreatitis in patients with acute abdominal pain. Thus selection of one of the three enzymes as diagnostic test of acute pancreatitis is to be based on considerations such as economy, methodological simplicity, possibility of automated assay and the time-consumption at the assay.
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PMID:Evaluation and comparison of cathodic trypsin-like immunoreactivity, pancreatic lipase and pancreatic isoamylase in the diagnosis of acute pancreatitis in 849 consecutive patients with acute abdominal pain. 371 97

Immunoreactive trypsin concentration and pancreatic lipase activity were measured in the sera of 33 patients with primary biliary cirrhosis. Immunoreactive trypsin was increased (above the normal range) in 16 (48%) and pancreatic lipase activity in 18 (55%) patients. Both enzymes were increased in 10 (30%) patients. Twenty four patients (73%) had an increase of either one or both enzymes. There was a significant correlation between immunoreactive trypsin and pancreatic lipase activity. This abnormality was not related to treatment with D-penicillamine, the age of the patients, the stage of the disease, or the severity of cholestasis. Thus most patients with primary biliary cirrhosis have increased pancreatic enzyme activity and immunoreactive trypsin concentration in their sera. These data are indicative of damage to the exocrine pancreas. The cause of this damage is as yet unknown.
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PMID:Serum immunoreactive trypsin and pancreatic lipase in primary biliary cirrhosis. 372 16

The purpose of the present study was to examine the adaptation of pancreatic lipase to the amount and nature of dietary lipids in the growing pig. Thirty pigs were distributed into three groups of 10 animals each. They were fed the same amount (1.5 kg/pig/day) of either diet C (3.5% lard, 3.5% sunflower oil, 67.7% starch), diet L (21% lard, 33.2% starch) or diet SO (21% sunflower oil, 33.2% starch) for 12 days. The diets were isoenergetic and isonitrogenous. Pancreas weight relative to live-weight was highest in group L. The pancreatic lipid content of the latter group exceeded that of groups C and SO by 53 and 39%, respectively. The pancreatic protein content was similar in the three groups. The specific lipase activity of pancreatic tissue (U per mg of protein) in group SO was about 1.6-fold higher than that of group L and about 3-fold higher than that of group C (31.9, 19 and 11.6, respectively). Specific amylase activity was higher in animals of group C than in those of the other two groups (C : 1689; L : 1112; SO : 984), whereas no difference was observed in chymotrypsin activity. Specific trypsin activity was lowest in group L. These results confirm the adaptation of pancreatic lipase and amylase to their respective substrates. Furthermore, it appears that lipase activity was more or less affected by the degree of unsaturation of lipids and that it was much higher for the same amount of triacylglycerols when the latter were rich in unsaturated fatty acids. The mechanisms involved have not been determined yet, but the possible physiopathological consequences of the increased pancreatic lipid content observed in pigs receiving triacylglycerol-rich diets (including especially saturated fatty acids) should be considered.
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PMID:Adaptation of pancreatic lipase to the amount and nature of dietary lipids in the growing pig. 382 2

The characteristics of the blood curves of alpha-amylase (SA), pancreatic lipase (SL) and immunoreactive trypsin (SIT) have been analyzed in a series of patients daily explored throughout the evolution of pancreatitis attacks; urines were also collected to estimate the amylase-creatinine clearance ratio (ACCR). The following results were obtained. a). The 3 enzymes profiles ran roughly parallel during an acute attack. b). SL rose far higher than SA at the onset of the attack but its decay displayed a shorter half-life than the latter; these features resulted in an absence of systematic difference between their times of return to normal levels at the end of the attack. c). SIT more closely correlated with SL than with SA. d). In common hospital practice, simultaneous SA and SL determinations were proving a more reliable help to diagnose pancreatitis attack than ACCR.
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PMID:Evolution of serum amylase, lipase and immunoreactive trypsin during pancreatitis attacks. 387 8

Serum immunoreactive trypsin (IRT) and pancreatic lipase have been measured in 59 patients with cystic fibrosis (age 1 month-27 years). Follow-up values were obtained from 49 patients. Their serum enzyme levels were compared to those of 120 healthy children of all age groups. Faecal fat excretion was determined in selected patients (n = 23) to elucidate the relationship between serum enzyme levels and pancreatic exocrine function. In cystic fibrosis IRT and lipase showed a very similar age-correlated pattern: in infancy levels were markedly elevated. During the following years the concentrations of both enzymes decreased rapidly and were found to be far below the normal range after the 10th year of life. Elevated enzyme levels in infancy as well as low levels in all age groups coincided with steatorrhea. Older patients (11-27 years) without severe pancreatic insufficiency however, had IRT and lipase levels in or above the normal range. In healthy children there was no age dependency of IRT levels, whereas in the first 12 months of life lipase levels were significantly lower than in later childhood.
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PMID:Serum immunoreactive trypsin and pancreatic lipase in cystic fibrosis. 404 29

A toxin which is lethal for two week old chicks has been recovered from strains of Escherichia coli O78:K80 of bovine and avian origin and from avian isolates of serogroups O2, O45 and O109. The toxin is heat-labile, antigenic, high in protein, inactivated by pronase, trypsin, amylase, and pancreatic lipase. The toxin may be precipitated by ammonium sulfate or TCA treatment from the supernatant obtained by repeated centrifugation of sonicated cells. Considerable purification has been obtained by column chromatography using Sepharose 6B.
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PMID:Studies on the chick-lethal toxin of Eecherichia coli. 427 Aug 9


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