Chemiluminescence light measurement units

Chemiluminescence intensities were obtained as follows xanthine oxidase (0.37 units/mL, 40 pL) was added to the mixture consisting of 20 mM Mops/0.2 M KCl (pH 7.2, 0.5 mL), 0.3 mM hypoxanthine (0.5 mL), and 25 mM probe in water at 25 °C, then the reaction mixture was placed in an Aloka Luminescence Reader BLR-301 and chemiluminescent intensity time curves were obtained at 25 °C. Immediately after xanthine oxidase was added, the chemiluminescence with maximum intensity was observed. The intensity of background chemiluminescence was measured before the addition of xanthine oxidase. Chemiluminescence spectra were obtained as follows the luminescence solution was placed in a JASCO FP-750DS spectrofluorometer and spectra were obtained without light-irradiation. 

Alkaline phosphatase-labeled probes are synthesized so that 18 bases are complementary to sequences on the arms of the bDNA. Three hybridization sites are located on each branch for a total binding capacity of 45 labeled probes per bDNA molecule. The alkaline phosphatase catalyzes the dephosphorylation of chemiluminescent substrate, dioxetane (Lumi-Phos Plus, Lumigen, Detroit, MI). The intensity of the light emission is measured with a plate luminometer as relative luminescent units. 

Measure the chemiluminescence intensity as described above. Plot the logarithm of luciferase content in the dilution series as a function of the logarithm of measured luminescence intensity (light units). Use an approximation function (usually... 

Light emitted by chemiluminescent substrate was expressed in relative light units (RLU). The time dependence of light intensity was measured and the peak intensity was converted into percent of inhibition relative to control. We expressed the results as total antioxidant potential, expressed as percent inhibition TAPcl = ((max RLUconiroi) - (max RLUsampie)) 100 / (max RLUcontroi). Figure 1 shows the correlation between sum of phenolic compounds... 

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