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Related to trypsin: chymotrypsin
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As part of the basic knowledge regarding gene studies for Centropomus poeyi, it was possible to obtain and registered two sequences for digestive enzymes, trypsin (TRY) and nonspecific cytosolic dipeptidase (CNP).
The enzymatic characterization by API-ZYM test system revealed alkaline-phosphatase, acidic-phosphatase, lipase, valine arylamidase, cystine arylamidase, naphthol-AS-BI-phosphohydrolase, [beta]-galactosidase, leucine arylamidase, and trypsin as positive enzymes produced by S.
The AMS, lipase and trypsin enzyme activities of the 30 h group in duodenum, jejunum and ileum were the highest (p<0.05), but AMS enzyme activities in duodenum and ileum was the best in the 24 h group (p<0.05).
At this point, samples were divided and immersed in two different decellularization solutions: Protocol I (5 mM EDTA, 50 mM TRIS, and 0.5% antibiotic) or Protocol II (5 mM EDTA, 0.05% trypsin, and 0.5% antibiotic).
Hydrolysis by commercial trypsin and chymotrypsin and enzymes in midgut extracts from each strain was evaluated by spectrophotometry at 404 nm, using a test tube assay with 1% azocasein as substrate and 10 m incubation at room temperature, as described by Garcia-Carreno et al.
Moreover, the selectivity of the active extracts toward HCV NS3/4A protease (viral protease) and not human serine proteases such as trypsin and chymotrypsin has been confirmed through investigating the inhibitory activity of these extracts and/or their isolated chemical constituents on Human recombinant Trypsin.
Bovine serum albumin (66kDa), ovoalbumin (45kDa), glyceraldehyde 3-phosphate dehydrogenase (36kDa), carbonic anhydrase (29kDa), trypsinogen (24kDa), trypsin inhibitor (20kDa) and lactoalbumin (14.2kDa) were used as molecular weight markers.
In the isolation of the commercial seeds and flour proteins analyzed, the affinity column with resin Sepharose CNBr 4B (Sigma, St Louis, United States) trypsin derivative was used, pre-equilibrated with buffer Tris-HCl 0.05 mol.
In penaeids, trypsin and chymotrypsin are the main proteinases, responsible for more than 60% of protein digestion (Galgani et al., 1984).
In this study, bovine pancreatic trypsin was immobilized by adsorption on the surface of nonmodified silica spheres (control) and silica spheres modified by silanization with aminopropyl triethoxysilane (APTS).
However, to verify that the activity of PIs is remained during processing, trypsin inhibition assay was prepared.