Modification of an assay for trypsin and its application for the estimation of enteropeptidase

Preiser, H.; Schmitz, J; Maestracci, D.; Crane, Robert K.

doi:10.1016/0009-8981(75)90025-x

Cited by 82 publications

(35 citation statements)

References 11 publications

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“…Pancreatic trypsin activity (EC 3.4.21.4) was quantified following the procedure of Preiser et al (Preiser et al, 1975). Because trypsin is secreted from the pancreas as an inactive zymogen, we also measured trypsin activity in small intestine contents of pythons between 12·h and 6 days after feeding.…”

Section: Pancreatic Trypsin Assaymentioning

confidence: 99%

Matched regulation of gastrointestinal performance in the Burmese python,Python molurus

Cox

Secor

2008

Journal of Experimental Biology

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SUMMARYIn Burmese pythons fasting and feeding cause dramatic regulation of gastric acid production and intestinal nutrient uptake. Predictably, other components of their gastrointestinal tract are similarly regulated with each meal. We therefore assessed the matched regulation of gastrointestinal performance by comparing the postprandial activities and capacities of gastric (pepsin), pancreatic (amylase and trypsin) and intestinal (aminopeptidase-N and maltase) enzymes, and intestinal nutrient uptake. Tissue samples were collected from pythons fasted and at 0.25, 0.5, 1, 2, 3, 4, 6, 10 and 15·days following their consumption of rodent meals equaling 25% of snake body mass. With feeding, pythons experience no significant change in stomach mass, whereas both the pancreas and small intestine doubled in mass. Feeding also triggered a depletion of gastric mucosal pepsinogen, a respective 5.7-and 20-fold increase in the peak activities of pancreatic trypsin and amylase, and a respective 2.3-and 5.5-fold increase in the peak activities of intestinal maltase and aminopeptidase-N. Enzyme activities peaked between 2 and 4·days postfeeding and returned to fasting levels by day·10. Independent of digestive stage, python intestine exhibited a proximal to distal decline in enzyme activity. For both sugars and proteins, intestinal capacities for enzyme activity were significantly correlated with nutrient uptake capacities. The concomitant postprandial upregulation of tissue morphology, intestinal nutrient transport rates and enzyme activities illustrate, for the python, the matched regulation of their gastrointestinal performance with each meal.

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Section: Pancreatic Trypsin Assaymentioning

confidence: 99%

Matched regulation of gastrointestinal performance in the Burmese python,Python molurus

Cox

Secor

2008

Journal of Experimental Biology

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“…Afterwards, the catheter was removed, the abdominal wall was sutured, and the ani mals were allowed to wake up and were allocated to restricted cages. Rats were also given an intravenous infusion of 1 ml/h/kg 0.15 M saline to prevent hypovolemia, as we had already found in a previous study [19], Every 6 h blood was drawn from the catheter to determine the endotoxin level by chromogenic assay [20], amylase by the method of Ceska et al [21 ] using the Phaedebas amylase test (Pharmacia Labo ratories, N.J., USA), and trypsin by the method of Preiser et al [22].…”

Section: Materials and M Ethodsmentioning

confidence: 99%

Bacterial Translocation in the Course of Acute Pancreatitis: Beneficial Role of Nonabsorbable Antibiotics and Lactitol Enemas

Marotta

Geng²,

Wu³

et al. 1996

Digestion

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Two-hundred Wistar rats were allocated to 4 groups. The groups, 3 representing our acute pancreatitis model induced by intrabiliary injection of a trypsin/enterokinase mixture, were studied as follows: (A) no treatment; (B) given a daily 30-ml enema with 20 mg/kg rifaximin; (C) given a daily 30-ml enema with 20 mg/kg rifaximin plus lactitol 0.5 g/kg, and (D) given a daily 30-ml enema with warm saline. A further group of healthy rats was given an intrabiliary injection of 0.15 ml saline. Sacrifices were made after 6,12,24,48 and 72 h of observation. Serial blood samples were drawn to measure pancreatic enzymes and endotoxin. At sacrifice, ascites, lymph nodes, pancreas, spleen, portal vein blood, arterial blood and bile were obtained for bacteriological culture. Both enema treatments brought about a significant improvement in survival. Enema treatments did not affect the serum level of pancreatic enzymes. A time-course increase in endotoxin level was observed in untreated rats. However, significantly decreased levels were observed after both enema treatments. Overall, ascites was the sample most frequently infected. Lymph nodes contiguous to the gut were found to be infected more frequently than those close to major vessels. The histological pancreatic damage was of a significantly lesser degree in both enema treatment groups. Virtually all severe necrotico-hemorrhagic pancreatic lesions were associated with bacterial infection. These data suggest that bacterial translocation plays a relevant role in the outcome of experimental necrotizing pancreatitis. Intra-abdominal spread and lymphatics seem to be the pathways most likely involved in such processes. Colonic cleansing by non-absorbable antibiotics and lactitol seems to exert a beneficial effect on the supervening infection of experimental necrotizing pancreatitis.

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“…Amylase activity was assayed by the modified method of Bernfeld (1955) using soluble Zulkowsky starch. After being activated with enterokinase, trypsinogen activity was determined by using a-N-benzoyl-DL-arginine-p-nitroanilide as a substrate (Erlanger, Kokowsky & Cohen, 1961) followed by the Bratton-Marshall reaction (Preiser, Schmitz, Maestracci & Crane, 1975). Enzyme reactions were carried out at 37 'C according to the method described by Saito et al (1980a) and enzyme activities were represented as international units with conversion factors of 9-25 nkat for 1 U of amylase and of 16-67 nkat for 1 U of trypsinogen.…”

Section: Measurementsmentioning

confidence: 99%

Suppression of secretagogue‐induced amylase secretion in pancreatic acini of cold‐exposed rats.

Habara

1989

The Journal of Physiology

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SUMMARY1. The influence of prolonged exposure to a low ambient temperature on the pancreatic exocrine function was investigated in rats. Amylase concentration in acini prepared from rats housed at 5 TC for 2 weeks was specifically and dramatically reduced. The enzyme activity relative to acinar DNA concentration was only 48 % of that of control acini obtained from rats reared at the thermoneutral temperature of 25 'C. Amylase content relative to acinar protein concentration also decreased by 35 %. In contrast, acinar trypsinogen content relative to protein concentration increased to 161 % of that of control acini. No comparable change was found in the parotid glands.2. In acini from cold-exposed rats, amylase release in response to cholecystokinin octapeptide or carbamylcholine was simultaneously reduced when expressed relative to acinar DNA or protein concentration and the dose-response curve shifted downward. However, when the secretary responsiveness of amylase was represented as a percentage of initial acinar enzyme content, the observed decrease disappeared and the dose-response curve was unaffected by cold exposure.3. Secretagogue-stimulated trypsinogen release was augmented in acini from coldexposed rats when expressed per acinar protein concentration. Conversely, its percentage release was slightly lowered but the release per acinar DNA concentration remained unaltered.4. Pancreatic insulin concentration normalized to tissue wet weight or protein concentration was unaffected by prolonged cold exposure but the plasma insulin concentration significantly decreased by 45% as compared with that of thermoneutral rats.5. Chronically administered exogenous insulin partially restored the decreased acinar amylase concentration in cold-exposed rats. The dose-response curve for amylase normalized by acinar DNA or protein content also tended to be shifted upward by insulin treatment. Acinar trypsinogen concentration in these rats was not significantly altered from that in cold-exposed, non-insulin-treated rats. Percentage release of each enzyme was decreased by exogenous insulin.6. Cold-induced suppression of pancreatic acinar amylase concentration, resulting in a proportional decrease in secretary responsiveness, was confirmed at the cellular level. Insulin deficiency at a low ambient temperature is likely to be a major cause of cold-induced suppression of amylase biosynthesis and its release via an insulin-pancreatic acinar axis.

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Modification of an assay for trypsin and its application for the estimation of enteropeptidase

Cited by 82 publications

References 11 publications

Matched regulation of gastrointestinal performance in the Burmese python,Python molurus

Matched regulation of gastrointestinal performance in the Burmese python,Python molurus

Bacterial Translocation in the Course of Acute Pancreatitis: Beneficial Role of Nonabsorbable Antibiotics and Lactitol Enemas

Suppression of secretagogue‐induced amylase secretion in pancreatic acini of cold‐exposed rats.

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