Search

Additional file 1: Figure S1. WS2 QDs FTIR. Figure S2. WS2 QDs fluorescence. Figure S3. A Cyclic voltammograms. B The histograms of 3 ��L WS2 QDs at different incubation temperatures (RT, 37 ��C and 4 ��C). Figure S4. A Cyclic voltammograms. B The histograms of 3 ��L WS2 QDs at different incubation times (30, 60, 90, 120 and 240 min) in RT incubation temperature. Figure S5. A Cyclic voltammograms. B The histograms of AuNPs deposition process at different cycles numbers (10, 15, 20, 25 and 30 cycles) in the range of ��� 0.5 to 0 V and the scanning rate of 0.05 V/S. Figure S6. A Cyclic voltammograms. B The histograms of immobilization of bacteriophage at different incubation temperatures (RT, 37 ��C and 4 ��C). Figure S7. A Cyclic voltammograms. B The histograms of phage at different incubation times (30, 60, 120, 180 and 300 min) at 4 ��C. Figure S8. A Cyclic voltammograms. B The histograms of target protein incubation temperature at RT, 37 ��C and 4 ��C. Figure S9. A Cyclic voltammograms. B The histograms of incubation time of protein at 30, 60, 120 and 180 min in 37 ��C.

Additional file 1: Table S1. Quantitative elemental analysis of rGO deposited GCE using EDX. Figure S1. A) Cyclic voltammogram of electrodeposition process of rGO; B) Cyclic voltammogram of final modified electrode which was recorded in the optimum experimental conditions. Figure S2. The optimization of rGO cycle number on the ECL intensities. A) The ECL curves for different cycle numbers of rGO (5, 10, 15, 20, 25) in GO solution (0.2 mg mL-1) (pH=8.5) with the same amount of CS:Ru mixture; B) The corresponding histograms, extracted from average ECL curves (n=3). Figure S3. Optimization of CS:Ru ration, A) The ECL curves for different proportions of CS/ Ru[(bpy)3] (0:5, 2:8, 4:6, 6:4, 8:2, CS:Ru); B) the ECL signal readouts for the proposed ratios of CS/ Ru[(bpy)3]. Figure S4. Optimization of incubation temperature of CS:Ru on the rGO modified GCE. A) The ECL plots for different temperatures of incubation (4, 10, 25, 30, 37, 45 °C); B) the related mean intensities. All the ECL measurements are obtained in PBS solutions (pH=8) and previously optimized parameters. Figure S5. Optimization of incubation time of CS:Ru on the rGO modified GCE at 25 °C. A) Effect of incubation time on ECL peak height (0, 30, 60, 90, 120, 150 minutes); B) the average ECL peak values obtained in different incubation times. Figure S6. Optimization of TPrA concentration: A) ECL signal readouts were obtained for different levels of TPrA in PBS solution (pH=8, 25 °C and 120 min); B) the related mean peak intensities of each point. Figure S7. Optimization of pH level. A) ECL plots obtained in PBS solutions at different pHs (5, 7.2, 7.6, 8.2, 8.6, 9); B) the correlated average signal intensities for each pH values. The experiments are performed in previously optimized conditions (25 °C, 120 min and 1.5 mL TPrA).

Ruta graveolens L. is a flavonoid-containing medicinal plant with various biological properties. In the present study, the effects of R. graveolens extract on aldehyde oxidase, a molybdenum hydroxylase, are investigated. Aldehyde oxidase was partially purified from liver homogenates of mature male guinea pigs by heat treatment and ammonium sulphate precipitation. The total extract was obtained by macerating the aerial parts of R. graveolens in MeOH 70% and the effect of this extract on the enzyme activity was assayed using phenanthridine, vanillin and benzaldehyde as substrates. Quercetin and its glycoside form, rutin were isolated, purified and identified from the extract and their inhibitory effects on the enzyme were investigated. R. graveolens extract exhibited a high inhibition on aldehyde oxidase activity (89-96%) at 100 microg/ml which was comparable with 10 microM of menadione, a specific potent inhibitor of aldehyde oxidase. The IC50 values for the inhibitory effect of extract against the oxidation of benzaldehyde, vanillin and phenanthridine were 10.4, 10.1, 43.2 microg/ml, respectively. Both quercetin and rutin at 10 microM caused 70-96% and 27-52% inhibition on the enzyme activity, respectively. Quercetin was more potent inhibitor than rutin, but both flavonols exerted their inhibitory effects mostly in a linear mixed-type.

Introduction: The aim of the present study was to assess the effects of vitamin E and selenium supplementation on serum paraoxonase (PON1) activity, lipid peroxidation and antioxidant defense in streptozotocin-induced diabetic rats. Methods: Thirty two female Sprague Dawley rats were divided into 3 groups: the control group (n=8) received a standard diet; streptozotocin (STZ)-induced diabetic rats (n=12), received corn oil and physiological solution; and vitamin E and selenium supplemented diabetic rats (n=12) were treated with oral administration of vitamin E (300 mg/kg) and sodium selenite (0.5 mg/kg) once a day for 4 weeks. Results: Significantly lower total antioxidant status (TAS), PON1and erythrocyte SOD activities and a higher fasting plasma glucose level were observed in the diabetic rats compared to the control. A significant increase in SOD and GPX activities in vitamin E and selenium supplemented diabetic group was observed after 5 weeks of the experiment. Compared to the normal rats, malondialdehyde (MDA) and oxidized LDL (Ox-LDL) levels were higher in the diabetic animals; however, these values reduced significantly following vitamin E and selenium supplementation. Conclusion: Vitamin E and selenium supplementation in diabetic rats has hypolipidemic, hypoglycemic and antioxidative effects and may slow down the progression of diabetic complications through its protective effect on PON1 activity and lipoproteins oxidation., BioImpacts; ISSN 2228-5660