Trypsin is a key protease related to digestion and absorption of proteins, which its inhibition must be studied when natural compounds, such as flavonoids, are used part alternative treatments for obesity diabetes mellitus type 2, since trypsin together with other pancreatic enzymes worked at small intestine. Considering that flavonoids good lipase amylase inhibitors, trypsin-flavonoids interac...

In human serum there are two protein fractions that are potent inhibitors to trypsin. These inhibitors travel with the a1-globulin and a2-globulin fractions when serum proteins are separated by electrophoresis (1-3). One ml of normal serum has sufficient amounts of trypsin inhibitor to neutralize the proteolytic effect of 1.15 (± 0.10) mg of crystalline trypsin. Approximately 90 per cent of the...

The crystal structure of a cyclic form of a mutant of bovine pancreatic trypsin inhibitor has been solved at 1.0 A resolution. The protein was synthesized by native chemical ligation and its structure is almost indistinguishable from the previously described recombinant form of the same mutant; however, the new loop containing the former termini became much better ordered.

Although recent evidence clearly indicates that trypsin inhibitors (TO and low protein digestibility are the major factors responsible for the pancreatic hypertrophic and growth inhibitory effects of raw soybeans, there was uncertainty regarding the biological threshold level of TI at which these biological effects occur. To obtain such data, dehulled defatted flakes (10% dietary protein) conta...

Wild growing mushrooms are a rich source of novel proteins with unique features. We have isolated and characterized trypsin inhibitors from two edible mushrooms, the honey fungus (Armillaria mellea) and the parasol mushroom (Macrolepiota procera), and from the poisonous death cap (Amanita phalloides). The trypsin inhibitors isolated: armespin, macrospin and amphaspin, have similar molecular mas...

BACKGROUND AND AIMS Endoprotease activation is a key step in acute pancreatitis and early inhibition of these enzymes may protect from organ damage. In vivo models commonly used to evaluate protease inhibitors require animal sacrifice and therefore limit the assessment of dynamic processes. Here, we established a non-invasive fluorescence imaging-based biomarker assay to assess real-time protea...

Trypsin (E.C.3.4.21.4) is a serine protease commonly used in proteomics for digestion of proteins. In the present study, the effect of nano-TiO2 on the conformation and catalytic activity of trypsin were studied. The thermal denaturation of trypsin has been investigated in the presence and absence of nano-TiO2 over the temperature range (293-373 K) at pH 3.0 and 7.25, using temperature scanning...