Pancreatic cancer is a malignant cancer with a high mortality rate. The amount of chymotrypsin C in pancreatic cancer cells is only 20% of that found in normal cells. Chymotrypsin C has been reported to be involved in cancer cell apoptosis, but its effect on pancreatic cancer cell migration is unclear. We performed cell migration scratch assays and Transwell experiments, and found that cell mig...

Variation in the inhibition of trypsin, chymotrypsin, and plasmin by serum was studied in 65 normal individuals and in 117 patients with a variety of diseases. It was shown that elevated inhibition for trypsin and chymotrypsin is associated with disease processes that bring about cellular destruction. Changes in the inhibition of trypsin and chymotrypsin were closely correlated with changes in ...

1. A trypsin and chymotrypsin inhibitor was isolated by extraction of chick-pea meal at pH8.3, followed by (NH4)2SO4 precipitation and successive column chromatography on CM-cellulose and calcium phosphate (hydroxyapatite). 2. The inhibitor was pure by polyacrylamide-gel and cellulose acetate electrophoresis and by isoelectric focusing in polyacrylamide gels. 3. The inhibitor had a molecular we...

Protein recovery under sonication treatment and autolysis, also protein hydrolysis progress during enzymatic hydrolysis (using trypsin and chymotrypsin) and autolysis (using endogenous enzymes) were investigated in Saccharomyces cerevisiae and Kluyveromyces marxianus. Crude protein content of dried yeast cells were 53.22% and 45.6% for S.cerevisiae and K.marxianus, respectively. After 96 hrs of...

Complexes of the Bowman-Birk soybean inhibitor with either trypsin or chymotrypsin and with both of these enzymes were isolated by gel atration. Amino acid analyses and molecular weight estimates by gel filtration were consistent with the formation of a 1: 1 molar complex between inhibitor and trypsin or chymotrypsin and a 1: 1: 1 molar complex composed of inhibitor, trypsin, and chymotrypsin. ...

Background: Hereditary pancreatitis is caused by mutations in human cationic trypsinogen. Chymotrypsin C is a proteolytic regulator of trypsinogen activation. Results: Clinically relevant trypsinogen mutations increase autoactivation in the presence of chymotrypsin C. Conclusion: Pathological trypsinogen activation in hereditary pancreatitis is dependent on chymotrypsin C. Significance: Therape...

A spectrofluorimetric investigation of the interactions between the subunits of the pancreatic bovine procarboxypeptidase A ternary complex was carried out after covalent insertion of a fluorescent probe at the active center of one of the constituent subunits. The specific insertion of an anthraniloyl group at the active center of subunit II free or bound to subunit I, after its conversion into...

PURPOSE Cockroach feces are known to be rich in IgE-reactive components. Various protease allergens were identified by proteomic analysis of German cockroach fecal extract in a previous study. In this study, we characterized a novel allergen, a chymotrypsin-like serine protease. METHODS A cDNA sequence homologous to chymotrypsin was obtained by analysis of German cockroach expressed sequence ...

1. Chymotrypsin is inactivated by N-acetyl-alpha-azaphenylalanine phenyl ester (phenyl N(2)-acetyl-N(1)-benzylcarbazate) in a stoicheiometric reaction. 2. The inactivation is reversible spontaneously (first-order rate constant is 1.2x10(-4)s(-1)) and accelerated by the presence of hydroxylamine. 3. Polymers based on polyacrylamide and carrying ligands containing the alpha-azaphenylalanine pheny...