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Nitrilase activity was measured using reverse-phase high-performance liquid chromatography by monitoring the decrease of mandelonitrile (substrate) or the increase of mandelic acid (product) at 210 nm.
Initiation of the reaction was carried out by the addition of NADH followed by monitoring the decrease in color intensity at 536 nm.
BVMO activity was measured by monitoring the decrease in absorbance of NADPH at 340 nm (εNADPH340 = 6.22 cm−1 mM−1) after addition of the substrate.
Enzyme activity was assayed at 30 °C by monitoring the decrease in the absorbance of NADH at 340 nm on an ultraviolet (UV /visible spectrophotometer (BioTek Instruments, Inc. Vermont, USA).
The adsorption time of Cu II), Cd II) and Ni II) ions onto the activated sludge and dried sludge was obtained by monitoring the decrease of metal ion concentration in aqueous solution with time.
The kinetics of the heme oxygenase reaction was studied by monitoring the decrease of the Soret band and the transient absorbance of verdoheme being an intermediate product in the formation of biliverdin.
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KmGRE2 activity was measured by monitoring the decreases in the absorbance at 340 nm caused by the reduction of aldehyde, or the increases in the absorbance caused by the oxidation of alcohol.
As in previous work, 23 degradation of the protein in response to light stress was assayed by simply monitoring the decrease in absorbance at 803 nm during incubation of RCs at room temperature in the light.
The reaction rate was determined by monitoring the concomitant decrease of NADH at 340 nm.
Complex IV activity was measured at 25 °C by monitoring the absorbance decrease of reduced cytochrome c at 550 nm.
β-carotene bleaching activity was determined by monitoring the absorbance decrease at 460 nm due to the disappearance of β-carotene (ε = 123.5 mM-1⋅ cm-1) [ 19].
More suggestions(17)
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by monitoring the mercury
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