2007
DOI: 10.1016/j.nutres.2006.12.011
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Ingestion of potato starch decreases chymotrypsin but does not affect trypsin, amylase, or lipase activity in the pancreas in rats

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Cited by 4 publications
(3 citation statements)
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“…Successful application of protease inhibitors to stimulate CCK release in humans most likely requires a combination of trypsin, chymotrypsin and elastase inhibition, 18 and inhibition of trypsin activity alone is probably not sufficient. [18][19][20] Furthermore, the inhibitors have to be resistant to the enzymatic activity of human gastric proteases. Our in vitro data show that PI2 indeed inhibited the action of trypsin, chymotrypsin and elastase under simulated gastric conditions, and data supplied by the manufacturers also confirmed that both the amount and inhibitory activity of PI2 in the product were not affected by processing of the minidrink.…”
Section: Discussionmentioning
confidence: 99%
“…Successful application of protease inhibitors to stimulate CCK release in humans most likely requires a combination of trypsin, chymotrypsin and elastase inhibition, 18 and inhibition of trypsin activity alone is probably not sufficient. [18][19][20] Furthermore, the inhibitors have to be resistant to the enzymatic activity of human gastric proteases. Our in vitro data show that PI2 indeed inhibited the action of trypsin, chymotrypsin and elastase under simulated gastric conditions, and data supplied by the manufacturers also confirmed that both the amount and inhibitory activity of PI2 in the product were not affected by processing of the minidrink.…”
Section: Discussionmentioning
confidence: 99%
“…The trypsin (TPS) activities in serum and tissue samples were assayed at 410 nm using the substrate N-benzoyl-DL-arginine p-nitroaniline hydrochloride (BAPNA) (A080-2-2, Nanjing Jiancheng Bioengineering Institute, Nanjing, Jiangsu, China) according to the manufacturer’s instructions [ 21 ]. TPS could react with BAPNA to release p-nitroaniline with a maximum absorption peak at 410 nm.…”
Section: Methodsmentioning
confidence: 99%
“…α Amylase activity in the tissue homogenate was determined by the production of maltose from soluble starch (Wako). 22) Briefly, the homogenate was diluted with cold 154 mM NaCl solution (1 vol:100 vol), and then the 50 µL homogenate dilution was mixed with 500 µL of 0.1% soluble starch solution and 450 µL of phosphate buffer at pH 7.4 in a test tube. The mixture was incubated for 10 min at 37 C in a water bath, and then the maltose concentration in the mixture was determined by the modified Nelson Somogyi method.…”
Section: Methodsmentioning
confidence: 99%