Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.1 (chymotrypsin)
10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Trypsin and chymotrypsin concentrations were determined in 180 spot stool specimens from 110 control patients in hospital. The lower limit of normality for each enzyme was placed at the 5% level: 95% of this population excreted feces containing more than 100 mug. of chymotrypsin and 30 mug. of trypsin per g. of feces. Chymotrypsin concentrations appeared to be a more reliable guide to pancreatic function than trypsin concentrations.Fecal chymotrypsin concentrations were subnormal in five patients with chronic pancreatitis, borderline in one patient with relapsing pancreatitis, subnormal in one patient after pancreatectomy, and subnormal in five of nine with carcinoma of the pancreas. Subnormal concentrations of fecal chymotrypsin were found in seven of 21 patients with chronic liver disease related to alcoholism, eight of 32 with a partial gastrectomy, three of 10 with adult celiac disease and five of 16 with psoriasis.It appears that the determination of fecal chymotrypsin concentrations provides a valuable screening test for pancreatic exocrine deficiency. However, normal results may be found in some patients with pancreatic disease and subnormal values may occur in some patients with other conditions.
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PMID:Fecal chymotrypsin and trypsin determinations. 555 Mar 76

To establish the diagnosis of acute pancreatitis the estimation of amylase in serum and urine, lipase and radio-immunoreactive trypsin in the serum are useful. Lipase estimations are more helpful than measuring amylase values. Trypsin-RIA-tests are increasingly important adults. But in chronic pancreatitis and inborn secretory insufficiencies of the pancreas these methods are less helpful. PABA-test, pancreolauryl-test (PLT), and the estimation of chymotrypsin in faeces are screening procedures, although their results correlate well amongst each other. As compared to the chymotrypsin estimation in faeces PABA test and PLT allow for some semiquantitative estimation of the secretory function and dynamics of the gland. The influence of malabsorption, liver and kidney diseases on these parameters is not yet quite clarified. Besides screening they are undoubtedly of value for judging the course and therapy of cystic fibrosis, Shwachman-syndrome, iatrogenic lesions by cytostatics (immunosuppressives and corticosteroids). Quantitative estimations of fat in faces and the pancreozymin test are no longer of significance.
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PMID:[Examination of pancreatic function in children with special reference to the PABA-test (author's transl)]. 616 2

An investigation of fecal chymotrypsin activity on spot fecal specimens was carried out in three groups of subjects, divided as follows: 45 healthy controls (group C); 36 patients with gastroenterological diseases of extrapancreatic origin (group VP); and 42 patients with chronic pancreatitis (group CP). Nineteen patients of group CP underwent pancreozymin-secretin and NBT-PABA tests. The following results, expressed as mg of chymotrypsin/g of feces, were obtained: C = 0.610 +/- 0.203; CP = 0.291 +/- 0.154, p less than 0.001; VP = 0.560 +/- 0.234. FCT showed a sensitivity rate of 78.5% and a specificity rate of 71.6%. The fecal output of chymotrypsin correlated well with the pancreatic secretion of chymotrypsin (r = 0.59, p less than 0.01) and with the percentage of recovery of urinary PABA (r = 0.44, p less than 0.05). We conclude that chymotrypsin assay by the described method on spot stool specimens is a simple, reliable technique which may be considered a good screening test for pancreatic insufficiency. The test will not detect minimal pancreatic disease or minimal pancreatic dysfunction.
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PMID:A single-specimen fecal chymotrypsin test in the diagnosis of pancreatic insufficiency: correlation with secretin-cholecystokinin and NBT-PABA tests. 633 29

Twenty-five patients with chronic pancreatitis and 25 patients with non-pancreatic abdominal disorders were investigated by Lundh and BT PABA/14C-PABA tests of pancreatic function. The following results emerged: (1) There was a strong positive linear relationship between mean trypsin activity (MTA) and mean chymotrypsin activity (MCA) in duodenal aspirates after a Lundh test meal. (2) There was a strong positive linear relationship between chymotrypsin activity measured with BTEE, or BT PABA as substrate. (3) There was a strong positive correlation between MTA, or MCA, in duodenal juice after a Lundh meal and urinary PABA recovery, or the PABA/14C excretion index (PEI) in patients with chronic pancreatitis, but not in controls. (4) There was no correlation between the pH of duodenal juice in Lundh tests and PABA recovery, or PEI, in patients with or without pancreatic disease. We conclude that the Lundh and BT PABA/14C-PABA tests are equally discriminatory methods of assessing pancreatic exocrine function. The rate limiting effect of pH on BT PABA hydrolysis reported in in-vitro studies does not affect the practical clinical value of the BT PABA/14C-PABA test.
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PMID:Relationship between PABA and Lundh tests: lack of influence of duodenal pH in vivo. 660 48

A comparative study using the oral test with chymotrypsin substrates p-(N-acetyl-L-tyrosyl)- and p-(N-benzoyl-L-tyrosyl) aminobenzoic acid (Ac-Tyr-PAB and Bz-Tyr-PAB) was carried out in 43 adults divided into four groups comprising controls (n = 18), chronic pancreatitis (n = 13), after acute pancreatitis (n = 7), and celiac sprue (n = 4), after separate administration of both derivatives and determination of PABA urinary output in 6 and 8 hours. Both derivatives were diagnostically comparable. The specificity of both derivatives in the investigated group in 6 and 8 hours was 100%, and test sensitivity in patients with chronic pancreatitis, was in 6 hours 90.9% for Ac-Tyr-PAB and 72.7% for Bz-Tyr-PAB, and 8 hours 81.8% for both compounds. Differentiation between the controls and the chronic pancreatitis group was better in Ac-Tyr-PAB, as adjudged by the sensitivity and significance of the Student t-test criterion.
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PMID:Comparative study of the estimation of exocrine pancreatic function using p-(N-acetyl-L-tyrosyl)- and p-(N-benzoyl-L-tyrosyl)aminobenzoic acid. 660 11

Two forms of alpha 1-proteinase inhibitor (alpha 1-PI) were characterized in the pancreatic juice of patients with chronic pancreatitis, one free form and one form complexed with a proteinase. This complex is probably present in minute amounts in normal pancreatic juice which contains mainly free alpha 1-PI. The proteinase bound to alpha 1-PI has been identified as chymotrypsin A and the inhibitory activity of the free form of alpha 1-PI has been demonstrated. These data underline the rapid conversion of human proteolytic zymogens into active enzymes and demonstrate the increase of this activation phenomenon in the juice of patients with chronic pancreatitis.
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PMID:Alpha 1-proteinase inhibitor in pure human pancreatic juice. Characterization of a complexed form in patients with chronic calcifying pancreatitis and its significance. 660 5

A newly developed photometric assay for determination of fecal chymotrypsin is compared with the titrimetric standard method. Correlation of both technics was highly significant with a correlation coefficient of r = 0.975. The precision of both methods is satisfactory, with a coefficient of variation of 3.7% for the photometric and 1.8% for the titrimetric method. The clinical value of fecal chymotrypsin tests and other "tubeless" function tests is discussed with special reference to diagnosis and prognosis of chronic pancreatitis.
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PMID:[Chymotrypsin activity in the stool: comparison of a new photometric technic and the standard titrimetric method]. 665 28

We studied the effect of bombesin (9 ng/kg X min for 30 min by intravenous infusion) on serum immunoreactive trypsin in healthy subjects and in chronic pancreatitis patients. Bombesin administration caused a marked and significant increase of serum immunoreactive trypsin concentration in healthy subjects. The increase occurred in the first 15 min after the beginning of bombesin infusion and persisted for the duration of the study (2 h). In patients with chronic pancreatitis, the increase was much less pronounced. In these patients, the integrated immunoreactive trypsin response to bombesin was significantly correlated with bicarbonate, lipase, and chymotrypsin outputs into the duodenum. The response of serum immunoreactive trypsin to bombesin stimulation seems to vary according to the degree of pancreatic exocrine dysfunction and to reflect the functional capacity of acinar cell mass.
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PMID:Effect of bombesin on serum immunoreactive trypsin in healthy subjects and in patients with chronic pancreatitis. 686 57

A sensitive and specific radioimmunoassay for human urinary kallikrein was developed, which allows tissue kallikrein determination in human urine, saliva, pancreatic juice, bile and sweat. In several body fluids a kallikrein-like antigen was found, but not in gastric juice and breast milk. According to gel filtration studies, complex formation of kallikrein with serum proteins or different molecular weight forms of kallikrein in serum and urine may be assumed. Pancreatic kallikrein secretion follows the same pattern after stimulation with secretin and cholecystokinin as trypsin and chymotrypsin in normal individuals. In chronic pancreatitis the kinetic behaviour remains unchanged with respect to the enzyme secretion, but the secretion of kallikrein is reduced to about 20%.
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PMID:Determination of kallikrein by radioimmunoassay in human body fluids. 690 40

Serum immunoreactive trypsin (IRT) response to secretin injection was studied in 13 patients with chronic pancreatitis with different degrees of exocrine dysfunction and in 10 control subjects. The maximal increase of serum IRT from basal values and the integrated trypsin output (ITO) after secretin administration were significantly correlated with the output of chymotrypsin into the duodenum during caerulein-secretin infusion (p < 0.01), but not with the output of lipase nor of bicarbonate. Serum IRT response to secretin stimulation was greater in 4 of the 5 patients with chronic pancreatitis with mild to moderate exocrine dysfunction than in the control group, suggesting an increased regurgitation of IRT into the blood stream by the pancreas, probably due to some degree of obstruction to pancreatic secretory flow in absence of severe acinar cell damage. Conversely, the response of serum IRT after secretin administration in 7 of the 8 patients with severe exocrine pancreatic deficiency was lower than in control subjects, probably because of the advanced distruction of the acinar pancreatic tissue. The response of serum IRT to secretin stimulation seems to vary following pancreatic function impairment and might reflect the degree of pancreatic exocrine dysfunction in chronic pancreatitis.
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PMID:Serum immunoreactive trypsin after secretin stimulation in chronic pancreatitis. 693 52


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