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
International journal of food microbiology, 91(3), 245-252 (2004-02-27)
We purified a carboxypeptidase (CPY) from the yeast of Kluyveromyces marxianus. This enzyme was purified 170 times from a soluble extract of 100000 x g. Purification consisted in a fractionated precipitation with ammonium sulfate and two chromatographic steps consisting of
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
Protease activity in gut of Daphnia magna: evidence for trypsin and chymotrypsin enzymes.
Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.
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