<p>The enzyme activity was assayed at various pH values in Britton & Robinson universal buffer in the range of pH 2–11 using DCPIP as electron acceptor. The enzymatic activity was assayed for 5 min at 35°C and the according pH using DCPIP as electron acceptor. All data represent the average of triplicate determinations ± standard derivation.</p
<p>The assay was performed at 53°C, pH 6.5 for 10 min using various concentrations of DPA. The data ...
<p>pH activity curves for WT and Δ2 to Δ10 mutant <i>α</i>Gal. % Activity is normalized against each...
<p>The enzymatic activity of Fpy1p was determined as described under <i>Experimental Procedures</i>,...
<p>The enzyme activity was assayed at various temperatures in the range of 5 to 60°C. All solutions ...
<p><sup>a</sup> All data represent the average of triplicate determinations ± standard derivation.</...
<p>The residual activity of the enzyme was assayed after incubation at various temperatures in the r...
<p>The pH stability of uninv (a), uninv2 (b) and M-inv2 (c) were tested at 37°C. The protein was inc...
<p>(a) Relative activity at different temperatures; and (b) relative activity at different pH. Relat...
<p>A: Native polyacrylamide gelelectrophoresis of the size exclusion chromatography step in combinat...
<p><sup>a</sup> Total protein was determined after cell disruption in the soluble fraction by the me...
<p>(A) pH optimum. The activities of GAD-C and GAD-V were determined in 50 mM citric acid-Na<sub>2</...
<p>Enzyme activities were determined in the presence of 3 mM UDP using the discontinuous apyrase act...
<p>A: Enzyme activities under different pH conditions. B: Enzyme activities of four AChEs under thei...
<p>The influence of detergents (A) and organic solvents with respective concentrations of 1% (w/v, v...
<p>The assay was performed in the presence of 10 mM NaTC. While the WT enzyme has a pH optimum of 5....
<p>The assay was performed at 53°C, pH 6.5 for 10 min using various concentrations of DPA. The data ...
<p>pH activity curves for WT and Δ2 to Δ10 mutant <i>α</i>Gal. % Activity is normalized against each...
<p>The enzymatic activity of Fpy1p was determined as described under <i>Experimental Procedures</i>,...
<p>The enzyme activity was assayed at various temperatures in the range of 5 to 60°C. All solutions ...
<p><sup>a</sup> All data represent the average of triplicate determinations ± standard derivation.</...
<p>The residual activity of the enzyme was assayed after incubation at various temperatures in the r...
<p>The pH stability of uninv (a), uninv2 (b) and M-inv2 (c) were tested at 37°C. The protein was inc...
<p>(a) Relative activity at different temperatures; and (b) relative activity at different pH. Relat...
<p>A: Native polyacrylamide gelelectrophoresis of the size exclusion chromatography step in combinat...
<p><sup>a</sup> Total protein was determined after cell disruption in the soluble fraction by the me...
<p>(A) pH optimum. The activities of GAD-C and GAD-V were determined in 50 mM citric acid-Na<sub>2</...
<p>Enzyme activities were determined in the presence of 3 mM UDP using the discontinuous apyrase act...
<p>A: Enzyme activities under different pH conditions. B: Enzyme activities of four AChEs under thei...
<p>The influence of detergents (A) and organic solvents with respective concentrations of 1% (w/v, v...
<p>The assay was performed in the presence of 10 mM NaTC. While the WT enzyme has a pH optimum of 5....
<p>The assay was performed at 53°C, pH 6.5 for 10 min using various concentrations of DPA. The data ...
<p>pH activity curves for WT and Δ2 to Δ10 mutant <i>α</i>Gal. % Activity is normalized against each...
<p>The enzymatic activity of Fpy1p was determined as described under <i>Experimental Procedures</i>,...
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