Studies Concerning the Effect of Glybenclamide, Streptozotocine and Insulin upon Pancreatic Juice Flow and Pancreatic Amylase and Lipase Activity, in Hens

2011 ◽  
Vol 4 (4) ◽  
pp. 417-418
Author(s):  
Iuliana Codreanu ◽  
Keyword(s):  
Pancreatic Juice ◽  
Lipase Activity ◽  
Pancreatic Amylase

scholarly journals Pancreatic amylase in chickens fed on soya-bean diets

1966 ◽  
Vol 20 (3) ◽  
pp. 421-437 ◽  
Author(s):  
S. Lepkovsky ◽  
T. Koike ◽  
M. Sugiura ◽  
M. K. Dimick ◽  
F. Furuta
Keyword(s):  
Pancreatic Juice ◽  
Nutritional Value ◽  
Amylase Activity ◽  
Soya Bean ◽  
Pancreatic Amylase ◽  
Protein Substrates ◽  
Intestinal Contents ◽  
Before And After ◽  
Methionine Supplementation

1. The action of raw and heated soya beans on pancreatic function was studied by measuring the amylase activity of the pancreases and intestinal contents of intact chickens and of chickens with ileostomies at fasting and after eating, before and after adaptation to heated and raw soya-bean diets, with a methionine supplement and without. 2. The concentration of amylase in the pancreases of 8-week-old chickens eating raw soya-bean diets was lower than that of those eating heated soya-bean diets. These chickens were deficient in methionine; supplementation of the raw soya-bean diet with methionine greatly increased the levels of amylase in the pancreases of such chickens; supplementation of the heated soya-bean diet with methionine increased the levels of amylase in pancreases to a smaller extent. 3. Methionine was less effective in increasing the amylase levels of the pancreases of 11-week-old chickens eating raw soya-bean diets, since at this age the deficiency of methionine was much less pronounced. 4. More amylase activity was found in intestinal contents of chickens eating raw soya-bean diets than in those eating heated soya-bean diets. 5. In vitro studies showed that fractions prepared from raw soya beans, all containing high levels of trypsin inhibitors, stabilized amylase activity despite the active proteolysis of other protein substrates in the same amylase-containing mixtures. 6. CaCl2 stabilized amylase activity in vitro in unactivated and activated pancreatic juice as such, and after additions of raw soya beans or their fractions before and after autoclaving. 7. The increased levels of amylase found in the intestinal contents of the chickens eating raw soya beans may represent greater secretion of amylase activity by the pancreas, stabilization of amylase activity by the raw soya bean, or both factors. Interpretation of measurements of amylase activity in the intestinal contents of chickens eating heated or raw soya beans is uncertain. 8. The bearing of this work on current views of the nutritional value of raw and heated soya beans is discussed.

scholarly journals Inherited Causes of Exocrine Pancreatic Dysfunction

1997 ◽  
Vol 11 (2) ◽  
pp. 145-152 ◽  
Author(s):  
Peter R Durie
Keyword(s):  
Cystic Fibrosis ◽  
Lipase Activity ◽  
Exocrine Pancreas ◽  
Adult Life ◽  
Pancreatic Function ◽  
Amylase Secretion ◽  
Pancreatic Amylase ◽  
Pancreatic Dysfunction ◽  
Secondary Phenomenon ◽  
Hereditary Conditions

The exocrine pancreas is functionally immature at birth. Protease function is probably adequate, but lipase activity approximates 5% to 10% of adult values in the newborn and remains low in infancy. Pancreatic amylase secretion is essentially absent at birth and remains low through the first years of life. Functional disturbances of the exocrine pancreas are less frequent in childhood than in adult life. Causes of pancreatic dysfunction in childhood can be divided in two general categories: hereditary conditions, which directly affect the pancreas; and acquired disorders, in which loss of pancreatic function is a secondary phenomenon. Most inherited causes of pancreatic dysfunction are due to a generalized disorder. Cystic fibrosis is, by far, the most common inherited cause of disturbed pancreatic function among Caucasian children. All other inherited causes of exocrine pancreatic dysfunction (eg, Johanson-Blizzard syndrome) are uncommon or rare.

Hepatobiliary and pancreatic clearance of circulating pancreatic amylase

1982 ◽  
Vol 243 (1) ◽  
pp. G21-G27 ◽  
Author(s):  
J. L. Rosenblum ◽  
B. K. Raab ◽  
D. H. Alpers
Keyword(s):  
Enzymatic Activity ◽  
Pancreatic Juice ◽  
Ribonuclease A ◽  
Pancreatic Enzymes ◽  
Amylolytic Activity ◽  
Significant Fraction ◽  
Pancreatic Amylase ◽  
Excellent Correlation ◽  
Intraarterial Infusion ◽  
Conscious Rabbit

The hepatobiliary and pancreatic uptake of pancreatic amylase was studied in the conscious rabbit. Four hours after intra-arterial injection of 125I-labeled porcine or rabbit pancreatic amylase, about 7% of the administered radioactive dose appeared in liver and bile, but less than 0.2% appeared in the pancreas and pancreatic juice. No amylolytic activity was detectable in bile, but a significant fraction of the acid-precipitable radioactive counts in bile comigrated with the injected amylase on gel autoradiography. Enzymatic activity appeared in bile after continuous intraarterial infusion of pancreatic amylase with excellent correlation between biliary and plasma amylase activities (r greater than or equal to 0.94). Only a small percentage (0.002%) of amylase delivered to liver, however, was excreted into bile. After intraduodenal instillation of radiolabeled pancreatic amylase or ribonuclease A, virtually none of the radioactivity appeared in the pancreas, and none in bile was acid precipitable. We conclude that a small but definite amount of the circulating pancreatic amylase is excreted intact into bile in the conscious rabbit. There is, however, no significant enterohepatic or enteropancreatic circulation of pancreatic enzymes.

Lipoprotein Lipase Activity in the Dog Pancreas and Pancreatic Juice.

1963 ◽  
Vol 113 (1) ◽  
pp. 127-132 ◽  
Author(s):  
J. I. Kessler ◽  
M. Finkel ◽  
D. A. Dreiling ◽  
H. D. Janowitz
Keyword(s):  
Lipoprotein Lipase ◽  
Pancreatic Juice ◽  
Lipase Activity ◽  
Lipoprotein Lipase Activity ◽  
Dog Pancreas

Rat lingual lipase: effect of proteases, bile, and pH on enzyme stability

1985 ◽  
Vol 249 (4) ◽  
pp. G496-G500 ◽  
Author(s):  
I. M. Roberts
Keyword(s):  
Gastric Juice ◽  
Pancreatic Juice ◽  
Lipase Activity ◽  
Enzyme Stability ◽  
Significant Loss ◽  
Duodenal Juice ◽  
Base Line ◽  
Initial Activity ◽  
Fat Digestion

In addition to initiating fat digestion in the stomach, lingual lipase may play a significant digestive role in the upper small intestine. By in vitro incubation techniques, the stability of rat lingual lipase at various physiological pH values, as well as the effects of pure proteases, rat gastric juice, bile, pancreatic juice, and mixed duodenal contents, on enzyme activity was explored. There were no changes in base-line activity of porcine pepsin, bovine carboxypeptidase-treated lipase, or heat-denatured proteases compared with controls after incubation at pH 2-6 at 37 degrees C for up to 1 h. In contrast, porcine trypsin-treated lipase demonstrated a significant loss from base-line activity to 59 +/- 12% (mean +/- SE) at pH 4, 34 +/- 11% at pH 6, and 41 +/- 4% at pH 8, and bovine chymotrypsin caused a loss in lipase activity to 11 +/- 7% at pH 8. Rat gastric juice containing 5,000 U pepsin reduced lipase activity to 17 +/- 5% of initial activity at pH 2 and to 45 +/- 3% at pH 4. Rat bile alone diminished activity only 35%, but rat pancreatic juice or mixed duodenal juice reduced lingual lipase activity to 1-12% of initial activity after 60 min at pH 6. Lingual lipase is particularly important in fat digestion in the stomach; however, its role in quantitative fat digestion under small intestinal conditions may be limited.

scholarly journals Assessment of Antiobesity Potential ofAchyranthes asperaLinn. Seed

2012 ◽  
Vol 2012 ◽  
pp. 1-7 ◽  
Author(s):  
Neerja Rani ◽  
Surendra Kumar Sharma ◽  
Neeru Vasudeva
Keyword(s):  
Lipase Activity ◽  
High Fat Diet ◽  
Ethanol Extract ◽  
Phytochemical Analysis ◽  
Pancreatic Amylase ◽  
High Fat ◽  
Saponin Content ◽  
Plasma Triacylglycerol

The present study was designed to evaluate the quality control parameters, quantitative phytochemical analysis (total phenols, total flavonoids, and total saponin content), and the antiobesity effect of ethanol extract ofAchyranthes asperaLinn. seed (EAA) by employingin vitroandin vivomodels. Inin vitrostudy, the inhibitory activity of EAA on pancreatic amylase and lipase was measured. Thein vivopancreatic lipase activity was evaluated by measurement of plasma triacylglycerol levels after oral administration of EAA along with lipid emulsion to Swiss albino mice. The EAA inhibited pancreatic amylase and lipase activity in vitro and elevations of plasma triacylglycerol level in mice. Furthermore, the antiobesity effect of EAA (900 mg/kg) was assessed in mice fed a high-fat diet with or without EAA for 6 weeks. EAA significantly suppressed the increase in body,retroperitoneal adiposetissue, liver weights, and serum parameters, namely; total cholesterol, total triglyceride, and LDL-cholesterol level. The anti obesity effects of EAA in high-fat-diet-treated mice may be partly mediated through delaying the intestinal absorption of dietary fat by inhibiting pancreatic amylase and lipase activity. Histopathological effects of EAA on the liver of mice were also assessed.

Regulation of pancreatic amylase and lipase gene expression by diet and insulin in diabetic rats

1994 ◽  
Vol 267 (4) ◽  
pp. G575-G583 ◽  
Author(s):  
A. Tsai ◽  
M. R. Cowan ◽  
D. G. Johnson ◽  
P. M. Brannon
Keyword(s):  
Gene Expression ◽  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Diabetic Rats ◽  
Differential Regulation ◽  
Complex Interaction ◽  
Dietary Control ◽  
Pancreatic Amylase ◽  
Lipase Gene ◽  
Dietary Regulation

Although insulin has been proposed to mediate the dietary regulation of pancreatic amylase, its interaction with diet in the regulation of amylase and lipase is not well understood and was examined in diabetic rats fed diets high in carbohydrate (HC), protein (HP), or fat (HF) and treated with insulin. Diabetes, independent of diet, decreased amylase content (97%; P < 0.0001) and mRNA (90%; P < 0.0001), but insulin only restored amylase content and mRNA to respective dietary control values. Diabetes, independent of diet, also increased lipase mRNA 1.6-fold (P < 0.004) but interacted (P < 0.0003) with diet on lipase content, resulting in opposite effects in HC- (increased 202%) and HF-diabetic rats (decreased 40%). Insulin partially restored lipase content and mRNA to respective dietary control values. Diet, independent of diabetes, regulated amylase content (P < 0.0001) and mRNA (P < 0.0003), which were three- to fourfold greater in HC- than in HF-fed rats, and lipase content (P < 0.001) and mRNA [rat pancreatic lipase 1 (rPL-1), P < 0.04; rPL-3, P < 0.0001], which were 1.8-fold greater in HF- than in HC- or HP-fed rats. Insulin failed to stimulate maximal amylase gene expression in HP- or HF-fed diabetic rats, suggesting that it is necessary, but not sufficient, for this dietary regulation. Differential regulation of lipase activity and mRNA by diet and insulin raises the possibility that lipase gene expression is regulated by a complex interaction of diet and insulin.

scholarly journals THE LIPASE ACTIVITY OF SHEEP PANCREATIC JUICE

1974 ◽  
Vol 59 (4) ◽  
pp. 351-359 ◽  
Author(s):  
G. Arienti ◽  
F. A. Harrison ◽  
W. M. F. Leat
Keyword(s):  
Pancreatic Juice ◽  
Lipase Activity
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