<p>(A) Trypsin. BAEE was hydrolyzed by trypsin to UV-absorbing product BA. Trypsin activity was measured as a slope of the UV absorbance change at <i>A</i><sub>253 nm</sub>. (B) Chymotrypsin. BTEE was hydrolyzed by chymotrypsin to UV-absorbing product BT. Chymotrypsin activity was measured as a slope of the UV absorbance change at <i>A</i><sub>256 nm</sub>. Data were averaged from three measurements.</p
<p>Trypsin and chymotrypsin were incubated respectively with different concentrations of SW-AT-1 at ...
using chromogenic substrates that are much smaller than physiological substrates. Methods: The hydro...
The absorbance data from the protease activity assay (results presented in Fig. 2C). Protease activi...
<p>(A) Trypsin (8 nM) was added to a mixture of 760 µM BAPNA and SW-AT-1 at 0 (□), 100 (○), 200 (Δ),...
<p>(A) Representative plot V/[S] of VpSP37, a single experiment is showed. The protease activity was...
The enzymolysis by α-chymotrypsin of the substrates, N-acetyl-L-tryptophane ethyl ester and N-acetyl...
A) Relative activity of bglTm throughout the assay at different temperatures. (purple cross) 29°C; (...
<p>(A) The nuclease activity was determined by mixing FLOS with serially diluted enzymes (1:10). The...
<p>The activity of heated trypsin following incubation with: (A) methylamines, (B) amino acids, (C) ...
UV scanning of a-chymotrypsin dissolved in neat glycerol and water showed no significant differences...
When crystalline trypsin was dissolved at various concentrations in pooled serum, the rates of hydro...
<p>To keep linearity, the assay time was fixed for 30 min and the temperature kept at 25°C.</p
Relative activity of (A) CalB (B) Commercial lipozyme CalB from Siam Victory Chemicals (C) SeqA and ...
considerably when compared to the measurement of the CONCENTRATION of an analyte (glucose, calcium, ...
†<p>Specific activity of partially deglycosylasted protease isoenzymes; ND: not determined.</p>#<p>I...
<p>Trypsin and chymotrypsin were incubated respectively with different concentrations of SW-AT-1 at ...
using chromogenic substrates that are much smaller than physiological substrates. Methods: The hydro...
The absorbance data from the protease activity assay (results presented in Fig. 2C). Protease activi...
<p>(A) Trypsin (8 nM) was added to a mixture of 760 µM BAPNA and SW-AT-1 at 0 (□), 100 (○), 200 (Δ),...
<p>(A) Representative plot V/[S] of VpSP37, a single experiment is showed. The protease activity was...
The enzymolysis by α-chymotrypsin of the substrates, N-acetyl-L-tryptophane ethyl ester and N-acetyl...
A) Relative activity of bglTm throughout the assay at different temperatures. (purple cross) 29°C; (...
<p>(A) The nuclease activity was determined by mixing FLOS with serially diluted enzymes (1:10). The...
<p>The activity of heated trypsin following incubation with: (A) methylamines, (B) amino acids, (C) ...
UV scanning of a-chymotrypsin dissolved in neat glycerol and water showed no significant differences...
When crystalline trypsin was dissolved at various concentrations in pooled serum, the rates of hydro...
<p>To keep linearity, the assay time was fixed for 30 min and the temperature kept at 25°C.</p
Relative activity of (A) CalB (B) Commercial lipozyme CalB from Siam Victory Chemicals (C) SeqA and ...
considerably when compared to the measurement of the CONCENTRATION of an analyte (glucose, calcium, ...
†<p>Specific activity of partially deglycosylasted protease isoenzymes; ND: not determined.</p>#<p>I...
<p>Trypsin and chymotrypsin were incubated respectively with different concentrations of SW-AT-1 at ...
using chromogenic substrates that are much smaller than physiological substrates. Methods: The hydro...
The absorbance data from the protease activity assay (results presented in Fig. 2C). Protease activi...