Diphenyl picrylhydrazyl (DPPH) free radical scavenging (IC 50 , µg/mL) was determined using UV-VIS spectrophotometer (Shimazu, UV-1800) with mobile phase methanol and water mixed online in the ratio of 85:15 (v/v), injected at a current speed of 0.8 mL/mins. Aliquots of the samples 1.0 mL were supplemented with 4.0 mL of the 0.05 mM DPPH solution in the dark place, and the mixture was well-blended and kept for 30 mins at ambient temperature. DPPH absorbance curve identified by UV-Vis spectrophotometer (Shimazu, UV-1800) at wavelength 517 nm (Andriana et al., 2019) (link). R 2 of the calibration curve was observed at 0.94.
Uv 1800
Manufactured by Shimadzu
Sourced in Japan, United States, Germany, Switzerland, China, United Kingdom, Italy, Belgium, France, India
The UV-1800 is a UV-Visible spectrophotometer manufactured by Shimadzu. It is designed to measure the absorbance or transmittance of light in the ultraviolet and visible wavelength regions. The UV-1800 can be used to analyze the concentration and purity of various samples, such as organic compounds, proteins, and DNA.
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Lab products found in correlation
Nicolet 6700, by Thermo Fisher Scientific (18 mentions)
Uv spectrophotometer, by Shimadzu (17 mentions)
Zetasizer nano z, by Malvern Panalytical (11 mentions)
Rf 6000, by Shimadzu (9 mentions)
S 4800, by Hitachi (9 mentions)
Jem 2100, by JEOL (9 mentions)
D8 advance, by Bruker (8 mentions)
2 2 diphenyl 1 picrylhydrazyl (dpph), by Merck Group (8 mentions)
Escalab 250xi, by Thermo Fisher Scientific (8 mentions)
Whatman filter paper, by Cytiva (7 mentions)
Uv vis spectrophotometer, by Shimadzu (7 mentions)
Nicolet is50, by Thermo Fisher Scientific (7 mentions)
No 1 filter paper, by Cytiva (6 mentions)
F 7000, by Hitachi (6 mentions)
Jem 2100f, by JEOL (6 mentions)
Gallic acid, by Merck Group (6 mentions)
Rf 5301pc, by Shimadzu (5 mentions)
Irtracer 100, by Shimadzu (5 mentions)
Uv 1650pc, by Shimadzu (5 mentions)
Jem 1400, by JEOL (5 mentions)
1 915 protocols using uv 1800
1
Antioxidant Activity via DPPH Assay
2
Quantitative Itopride Hydrochloride Analysis
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Itopride hydrochloride content in each tablet formulation was assessed using UV-Spectrophotometer (UV-1800, Shimadzu, Japan) with the help of reported methods 28,35&36 . Ten compacted ITP tablets of each formulation were randomly selected and crushed into mortar and pestle for their drug content. Take accurately weighed crushed powder equivalent to weight of single tablet (350 mg) and transferred to a 100 mL volumetric flask containing 50 mL of 0.1 N (1)
hydrochloric acid (HCl). Then, the flask was sonicated (Digital Ultrasonic Cleaner-Supersonic X3, Germany) for 10 min and volume was made up with the same solvent. The sample was subjected to analysis after filtration and appropriate dilution to 25 µg/mL and detection was performed at a wavelength of 258 nm using spectrophotometer (Shimadzu UV 1800, Japan)
hydrochloric acid (HCl). Then, the flask was sonicated (Digital Ultrasonic Cleaner-Supersonic X3, Germany) for 10 min and volume was made up with the same solvent. The sample was subjected to analysis after filtration and appropriate dilution to 25 µg/mL and detection was performed at a wavelength of 258 nm using spectrophotometer (Shimadzu UV 1800, Japan)
3
Quantifying Phenolics and Flavonoids
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The total phenolics content was determined using the Folin–Ciocalteu method with slight modifications (Li et al., 2021 ). In brief, 2.5 mL Folin–Ciocalteu reagent was prepared and added to a 1 g sample. Then 1.5 mL sodium carbonate solution (75 g/L) was added, and the resulting mixture was vortexed for 1 min. After the mixture had been kept at room temperature in the dark for 40 min, the absorbance at 760 nm was read using a UV spectrophotometer (UV-1800; Shimadzu, Kyoto, Japan). Gallic acid was used as a control. The total phenolics content was expressed as the gallic acid equivalent (GAE).
The total flavonoids content was determined by the AlCl3 colorimetric method (Mokrani et al., 2019 (link)) with minor modifications. In brief, a 1 g sample was added to 10 mL of 70% ethanol. The resulting mixture was sonicated at 25 °C for 40 min and then centrifuged at 5000 g for 10 min, and the supernatant was collected. Next, 100 µL supernatant and 30 µL of 5% NaNO2 were mixed. The mixture was allowed to react for 5 min before 30 µL of 10% AlCl3 was added and was then vortexed and incubated for 6 min. Then 200 µL NaOH (1 mol/L) was added, and the mixture was allowed to react for 5 min. The absorbance at 510 nm was measured by a UV spectrophotometer (UV-1800; Shimadzu, Kyoto, Japan). The total flavonoids content was expressed as the rutin equivalent.
The total flavonoids content was determined by the AlCl3 colorimetric method (Mokrani et al., 2019 (link)) with minor modifications. In brief, a 1 g sample was added to 10 mL of 70% ethanol. The resulting mixture was sonicated at 25 °C for 40 min and then centrifuged at 5000 g for 10 min, and the supernatant was collected. Next, 100 µL supernatant and 30 µL of 5% NaNO2 were mixed. The mixture was allowed to react for 5 min before 30 µL of 10% AlCl3 was added and was then vortexed and incubated for 6 min. Then 200 µL NaOH (1 mol/L) was added, and the mixture was allowed to react for 5 min. The absorbance at 510 nm was measured by a UV spectrophotometer (UV-1800; Shimadzu, Kyoto, Japan). The total flavonoids content was expressed as the rutin equivalent.
4
Spectrophotometric Assay of Oxidative Markers
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The MDA and rGSH levels in SH-SY5Y neuronal cells (106 cells in per ml) were spectrophotometrically (UV-1800, Shimadzu, Kyoto, Japan) measured at 532 and 412 nm by using the methods of Placer et al.52 (link) and Sedlak and Lindsay53 (link) as described in a previous study, respectively21 (link). The rGSH level was expressed as μg/g protein For measuring GPx activity, a spectrophotometric method of Lawrence and Burk54 (link) was used in the cells as described in previous studies29. The results of GPx was expressed as international unit (IU) of rGSH oxidized/min/g protein. The total protein in the supernatant was spectrophotometrically (Shimadzu UV-1800) assessed using Bradford reagent at 595 nm.
5
Spectrophotometric Analysis of Lipid Peroxidation and Glutathione in DBTRG Cells
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The LipPX and rGSH levels in DBTRG neuronal cells (10 6 cells in per ml) were spectrophotometrically (UV-1800, Shimadzu, Kyoto, Japan) measured at 532 and 412 nm by using the methods of Placer et al. (1966) and Sedlak and Lindsay (1968) as described in a previous study, respectively (Ertilav et al. 2018; Ataizi et al. 2019 ).
The rGSH level was expressed as μg/g protein.
For assaying GSHPx activity, a spectrophotometric method of Lawrence and Burk (1976) was used in the cells as described in previous studies (Ertilav et al. 2018; Ataizi et al. 2019) . The results of GSHPx activity was expressed as international unit (IU) of rGSH oxidized/min/g protein. The total protein content in the cell suspension was spectrophotometrically (Shimadzu UV-1800) assessed using Lowry's reagent.
The rGSH level was expressed as μg/g protein.
For assaying GSHPx activity, a spectrophotometric method of Lawrence and Burk (1976) was used in the cells as described in previous studies (Ertilav et al. 2018; Ataizi et al. 2019) . The results of GSHPx activity was expressed as international unit (IU) of rGSH oxidized/min/g protein. The total protein content in the cell suspension was spectrophotometrically (Shimadzu UV-1800) assessed using Lowry's reagent.
6
Assay of PHA Synthase Activity
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Assay of PHA synthase activity was carried out according to the methods described in literature (Miyake et al., 1997; Valentin and Steinbuchel, 1994) . The assay mixtures (1 ml) contained 50 µl of 50 mM DL-β-hydroxybutyryl coenzyme A lithium salt (final concentration 2.5 mM) (Sigma-Aldrich, Cat No: H0261), 50 µl of 20 mM 5, 5`-dithio-bis (2-nitrobenzoic acid) (final concentration 1 mM) (DTNB, Wako pure chemicals, Japan, Cat No: 047-16401) in 870 µ1 of 1M Tris-HCl buffer. The reaction was started by addition of 30 µl of crude enzyme. The optical density of the thiobenzoate anion resulting from the reaction of CoA and DTNB was measured at 412 nm for 1 min at room temperature using spectrophotometer (UV-1800, Shimadzu, Japan). Protein concentration was determined by Bradford protein assay (Bio-Rad, Hercules, CA, USA) and bovine serum albumin (Pierce, Rockford, IL, USA) as the standard at 595 nm using spectrophotometer (UV-1800, Shimadzu, Japan).
7
Measuring RNase and Insulin Refolding Activity
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RNase oxidative refolding activity was measured by means of RNase-catalyzed hydrolysis of cytidine 2′,3′-cyclic monophosphate (cCMP; Sigma–Aldrich) [18,19] . Reduced and denatured RNase (10 μM, Sigma–Aldrich), prepared as described previously [12] (link), was incubated with each recombinant PDIL (1 μM) in 100 mM Tris–HCl (pH 8.0) containing 1 mM GSH, 0.2 mM glutathione disulfide (GSSG), and 2 mM EDTA at 28 °C for the times indicated in the figures, and the reactions were stopped by the addition of N-ethylmaleimide (final concentration, 2 mM). After the addition of 2 mM cCMP, hydrolysis of cCMP resulting from the restoration of RNase activity was measured as an increase in absorbance at 296 nm by means of a spectrophotometer (UV-1800, Shimadzu).
Insulin disulfide reduction assays [20] (link) were performed using dithiothreitol (DTT) or GSH as an electron donor. Insulin (125 μM, Sigma–Aldrich) was incubated with each recombinant PDIL (0.5 μM) in 100 mM phosphate buffer (pH 8.0) containing 2 mM EDTA at 28 °C for the times indicated in the figures, either in the presence of 160 μM DTT or in the presence of 0.2 mM GSSG and GSH (1, 2, or 4 mM). The increase in turbidity accompanying reduction of the intramolecular disulfide bonds of insulin was monitored at 650 nm by means of a spectrophotometer (UV-1800, Shimadzu).
Insulin disulfide reduction assays [20] (link) were performed using dithiothreitol (DTT) or GSH as an electron donor. Insulin (125 μM, Sigma–Aldrich) was incubated with each recombinant PDIL (0.5 μM) in 100 mM phosphate buffer (pH 8.0) containing 2 mM EDTA at 28 °C for the times indicated in the figures, either in the presence of 160 μM DTT or in the presence of 0.2 mM GSSG and GSH (1, 2, or 4 mM). The increase in turbidity accompanying reduction of the intramolecular disulfide bonds of insulin was monitored at 650 nm by means of a spectrophotometer (UV-1800, Shimadzu).
8
Sulfide Quantification and OD600 Measurement
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Sulfides were measured as previously described (Cline, 1969 (link); Kleinsteuber et al., 2008 (link)) against a blank control. Previously frozen samples were thawed and mixed with 4 ml water and 0.4 ml of Cline’s solution. The mixtures were stored in the dark for 20 min before photometric measurement on an UV-1800 (Shimadzu, Germany) at 670 nm. Due to the high concentrations of sulfides, samples were diluted before measurement. Optical densities of cell suspensions were determined on an UV-1800 (Shimadzu, Germany) at 600 nm. 1 ml culture solution was transferred via syringe into a cuvette filled with a few mg of Na-dithionite, closed with parafilm and shaken until dissolved and then measured using water as control.
9
Quantifying Superoxide and Nitric Oxide in Soybean Seeds
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Superoxide (O2•−) content in each sample was determined by the method of Chaitanya and Naithani [38 (link)]. One hundred milligram of soybean (24 h soaked) seeds from different treatments were homogenised with chilled sodium phosphate buffer (0.2 M; pH 7.2) containing diethyldithiocarbamate (10–3 M) to inhibit the activity of superoxide dismutase. After centrifugation of homogenate at 10,000 rpm on 4 °C for 15 min, the O2•− content was measured in the supernatant by its capacity to reduce nitroblue tetrazolium (NBT, 2.5 × 10−4 M) with a UV–Vis spectrophotometer (UV-1800, Shimadzu, Kyoto, Japan). The absorbance was taken at 540 nm and the content was expressed as μmol O2•−g−1 fresh weight (FW) of seeds by using the molar absorption coefficient of 12.8 mM−1 cm−1.
Nitric oxide (NO) content was measured by Greiss reagent (1% sulphanilamide + 0.1% N-1-napthylethylenediamine dihydrochloride in 5% H2PO4 solution) as described in the method of Zhou et al. [39 (link)]. It was estimated as absorbance of the sample at 540 nm with a UV-Vis spectrophotometer (UV-1800, Shimadzu, Japan) using a standard curve prepared with NaNO2. The NO content was expressed in nmol NO g−1 fresh weight of seeds.
Nitric oxide (NO) content was measured by Greiss reagent (1% sulphanilamide + 0.1% N-1-napthylethylenediamine dihydrochloride in 5% H2PO4 solution) as described in the method of Zhou et al. [39 (link)]. It was estimated as absorbance of the sample at 540 nm with a UV-Vis spectrophotometer (UV-1800, Shimadzu, Japan) using a standard curve prepared with NaNO2. The NO content was expressed in nmol NO g−1 fresh weight of seeds.
10
Quantifying Antioxidants in Yogurt
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The preparations of yogurt samples were carried out according to Trigueros et al. (2014) (link) with some modifications. We extracted 2.0-g samples of yogurt using 60 mL of 60% (vol/vol) acidified ethanol in water with ultrasonic treatment at 200 W for 2 h twice, followed by vacuum filtration. The 2 filtrates were combined, subjected to rotary evaporation at 50°C, and centrifuged at 3,570 × g for 10 min at 4°C. The supernatants were diluted to 25 mL for measurement. The TPC was determined using the Folin-Ciocalteu method (Yadav et al., 2018) (link) by measuring the absorbance at 760 nm using a spectrophotometer (UV-1800, Shimadzu). The results were expressed as milligram of GAE per gram of yogurt. The TAC was determined using the pH differential method (Liu et al., 2004 (link)) on a spectrophotometer (UV-1800, Shimadzu). The results were expressed as microgram of C3GE per gram of yogurt.
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