N-Benzoyl-L-tyrosine p-nitroanilide (BTPNA) is used as a substrate to identify, differentiate and characterize serine carboxypeptidase(s) and various proteases.
Insect biochemistry and molecular biology, 31(4-5), 415-423 (2001-02-27)
Protease activities in the secreted saliva, salivary glands and midgut of the green mirid, Creontiades dilutus, were investigated. The saliva and salivary glands had more protease activity than the midgut, but no differences in protease activity levels were detected between
In assaying chymotrypsin inhibition by the soybean Bowman-Birk inhibitor, two sequences of mixing the reactants were tried: adding the substrate last (s-last test) or adding the enzyme last (e-last test). The inhibition values obtained from the s-last test were either
Proteases in egg, miracidium and adult of Fasciola gigantica. Characterization of serine and cysteine proteases from adult.
Journal of separation science, 30(17), 3069-3076 (2007-10-11)
The preparation and optimization of a new monolithic chymotrypsin bioreactor for online protein digestion is described. Silica monolithic supports have been activated with epoxide functionalities following an optimized in situ procedure and used for covalent immobilization of chymotrypsin in one-step
Journal of immunology (Baltimore, Md. : 1950), 147(6), 1912-1919 (1991-09-15)
The effects of carbobenzyloxy-leucine-tyrosine-chloromethylketone (zLYCK), an inhibitor of chymotrypsin, were investigated on the activation pathways of the human neutrophil respiratory burst. At 10 microM zLYCK, a parallel inhibition was observed of superoxide production stimulated with the chemo-attractant FMLP and of
Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.
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