N-Benzoyl-L-tyrosine p-nitroanilide (BTPNA) is used as a substrate to identify, differentiate and characterize serine carboxypeptidase(s) and various proteases.
Both activity and stability of alpha-Chymotrypsin (ChT) are substantially enhanced in the microdomains of laurylated or benzylated derivatives of poly(ethylenimine). EPR data revealed that the enhancement in activity of ChT is due to increase in the polarity of the microenvironment
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
Protease activity in gut of Daphnia magna: evidence for trypsin and chymotrypsin enzymes.
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
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
Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.
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