Digestive enzymes, inhibition

Cytotoxic activity. Ethanol (90%) extract of the dried plant, in cell culture administered at a concentration 0.25 mg/mL, was active on human lymphocytes. The extract was active on Veto cells, effective dose (EDjo 0.15 mg/mL Chinese hamster ovary (CHO) cells, EDjq 0.575 mg/mL and Dalton s lymphoma, EDjo 0.6 mg/mL "" ". Water extract of the dried gum, in cell culture at a concentration of 500 pg/mL, produced weak activity on CA-mammary-microalveolar cells "° L Digestive enzyme inhibition. Asafoetida, administered orally to rats at a dose of 2500 mg% for 8 weeks, decreased the levels of... 

The nephrotoxic amino acid, lyskioalanine [18810-04-3] formed upon alkaline treatment of proteki, was reported ki 1964 (108). Its toxicity seems to be mitigated ki proteki ki that it is not released by normal digestion (109). Naturally occurring new amino acids, which can be classified as protekiaceous or non-protekiaceous, can, as ki the case of those from some legumes, show a remarkable toxicity (110). Eor the details of amino acid toxicity, see reference 6. Enzyme inhibition by amino acids and thek derivatives have been reviewed (111). 

Diabetic patients have reduced antioxidant defences and suffer from an increased risk of free radical-mediated diseases such as coronary heart disease. EC has a pronounced insulin-like effect on erythrocyte membrane-bound acetylcholinesterase in type II diabetic patients (Rizvi and Zaid, 2001). Tea polyphenols were shown to possess anti-diabetic activity and to be effective both in the prevention and treatment of diabetes (Choi et al, 1998 Yang et al, 1999). The main mechanism by which tea polyphenols appear to lower serum glucose levels is via the inhibition of the activity of the starch digesting enzyme, amylase. Tea inhibits both salivary and intestinal amylase, so that starch is broken down more slowly and the rise in serum glucose is thus reduced. In addition, tea may affect the intestinal absorption of glucose. 

In addition to proteases, other inhibitors reduce the activity of amylase and other digestive enzymes (Ishimoto et al, 1999). Many varieties of beans produce a glycoprotein that complexes with and inhibits a-amylase (Mirkov et al, 1995). The amylase inhibitors are non-competitive and thermostable (Gallaher and Schneeman, 1986) and, unlike protease inhibitors, do not elicit heightened secretion of amylase (Toskes, 1986). Although over-expression... 

There is evidence that protease inhibitors selectively regulate the activity of specific digestive enzymes at the level of gene expression (Rosewicz et al., 1989). Specifically, soybean trypsin inhibitor increases secretion of proteases, including a form of trypsin that is resistant to inhibition but does not cause an increase in amylase secretion. Although the relationships between protease inhibitors and exocrine pancreatic secretion have received the most attention, pancreatic secretion is increased when potato fiber is added to the diet (Jacob et al., 2000), although the mechanism and signaling pathway have not been elucidated. 

CARMONA A (1996) Tannins thermostable pigments which complex dietary proteins and inhibit digestive enzymes. Latinoam Nutr. 44 31S-35S. 

Cholecystokinin Endocrine cells in mucosa of duodenum Breakdown products of lipid and, to a small extent, protein digestion in duodenum Inhibits gastric emptying and gastric secretion stimulates contraction of gallbladder stimulates secretion of digestive enzymes from pancreas... 

Mechanism Bind to digestive enzymes of herbivores variable molecules, specific for proteins Inhibit pathogen s exo-enzyme system... 

Blytt, H. J., Guscar, T. K., and Butler, L. G. (1988). Antinutritional effects and ecological significance of dietary condensed tannins may not be due to binding and inhibiting digestive enzymes. Journal ofChemicalEcology 14,1455. 

In general, ethanol in low to moderate amounts, is relatively benign to most body systems. A moderate amount of ethanol causes peripheral vasodilation, especially of cutaneous vessels, and stimulates the secretion of salivary and gastric fluids the latter action may aid digestion. On the other hand, ethanol consumption in high concentrations, as found in undiluted spirits, can induce hemorrhagic lesions in the duodenum, inhibit intestinal brush border enzymes, inhibit the uptake of amino acids, and limit the absorption of vitamins and minerals. In addition, ethanol can reduce blood testosterone levels, resulting in sexual dysfunction. 

The presence of PCR primers in restriction digests, which inhibit the restriction enzyme. 

The cholesterol-lowering properties of dietary plant sterols have been known for decades (Best et al., 1954 Peterson, 1951 Poliak, 1953), due specifically to reductions in cholesterol absorption. Inverse correlations between plant sterol intake and cholesterol absorption have been reported in animals (Carr et al., 2002 Ntanios and Jones, 1999) and humans (Ellegard et al., 2000). The exact mechanism by which plant sterols inhibit cholesterol absorption is unclear, and several mechanisms of action have been proposed, including (1) competition with cholesterol for solubilization in micelles within the intestinal lumen, (2) cocrystallization with cholesterol to form insoluble crystals, (3) interaction with digestive enzymes, and (4) regulation of intestinal transporters of cholesterol. 

The cereal dual function a-amylase/trypsin inhibitor proteins are cysteine-rich, disulphide-rich, double-headed, 13-16 kDa, dual function inhibitor proteins that inhibit both of the digestion enzymes a-amylase and trypsin [290-325] (Table 11). Thus the Zea (com) member of this family, com Hageman factor inhibitor (CHFI), is a double-headed 14 kDa protein that inhibits a-amylase and the serine proteases trypsin and blood clotting Factor Xlla [323-324] (Table 11). The structures of the bifunctional a-amylase/trypsin inhibitor proteins from Eleusine (ragi) (RBI) [292-295] and Zea (com) (CHFI) [325] have been determined. These proteins are structurally similar to the lipid transfer proteins, being composed of a bundle of 4 a-helices together with a short [3-sheet element connected by loops, the a-amylase- and protease-inhibitory domains being separately located [325]. 

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