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356 protocols using uv 2600 spectrophotometer

1

Earthworm Coelomocyte Antioxidant Analysis

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After being cultured for 24 h, the earthworm coelomocyte fluid was centrifuged (3500 RPM, 5 min). The supernatant was poured out, and washed twice with normal saline under the same centrifugation conditions. The coelomocytes were treated with 20% amplitude ultrasound and centrifugated at 5000 RPM for 5 min at 4 °C. Then the supernatant was collected to determine the total SOD activity, CAT activity, GSH content, and MDA level. According to the kit instructions (Nanjing Jiancheng Biological Engineering Institute, Nanjing, China), the total SOD activity, GSH content, and MDA level were calculated by using a UV-2600 spectrophotometer (Shimadzu, Kyoto, Japan) to measure A550, A405 and A532, respectively.
CAT activity was evaluated by measuring the absorbance change rate of H2O2 at 240 nm [21 (link)]. 300 μL supernatant was quickly mixed with 2.7 mL hydrogen peroxide (10 mM, diluted with normal saline), and then A240 was recorded by using a UV-2600 spectrophotometer (Shimadzu, Kyoto, Japan). Using ultrapure water as a reference, the changes in A240 were measured every 30 s within 3 min. After the measurement, the measured data were drawn as a scatter plot, and linear fitting was performed. The slope of the line was the change rate of H2O2 absorbance (the X axis was the measurement time, and the Y axis was the value of A240 every 30 s).
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2

Spectrophotometric Analysis of Hemoglobin Oxygenation

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The (HbII-HbIII)-O2 titrations with K3Fe(CN)6 were recorded using a SHIMADZU UV-2600 spectrophotometer with pH and spectral ranges from 4 to 9, and from 350 to 750 nm, respectively. The (HbII-HbIII)-O2 protein sample (20μM) was prepared in PBS (50mM K2HPO4/50mM KH2PO4) with a pH range of 4 to 9. Each sample was then titrated with a 40mM K3Fe(CN)6 solution by adding aliquots of 0.2μL to the samples until no notable change was observed. To study the effect of the crystallization conditions on (HbII-HbIII)-O2 in solution (5.0 M Sodium formate buffered to pH with sodium acetate for pH 4–7 and Tris-HCl for pH 8–9), an aliquot of (HbII-HbIII)-O2 was transferred to a 2.0 M solution of sodium formate at pH 4.6 and monitored through time with a SHIMADZU UV-2600 spectrophotometer. This solution is 60% less concentrated than the crystallization condition to avoid sample precipitation.
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Synthesis and Characterization of Citrate-Coated Silver Nanoparticles

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Five milliliters of 0.01 M AgNO3 was heated to boiling. To this solution, 0.5 ml of 1% trisodium citrate (pH 5.0) was added drop by drop. During the process, the solution was mixed vigorously and heated until the change in color was evident (brownish-yellow). Then, it was removed from the heating device and stirred until cooled to room temperature. After synthesis, the particles were washed with distilled water twice and suspended in 1× phosphate-buffered saline (PBS, pH 7.0) for storage and further experiments.
The citrate-coated AgNPs were characterized using SPR pattern under UV–vis spectra ranging from 300 to 700 nm using a Shimazu UV-2600 spectrophotometer. The average hydrodynamic diameter and stability of biogenic LAgNPs were determined using DLS and zeta potential studies by Microtrac's dynamic light scattering model Nanotrac.
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Biogenic Silver Nanoparticle Characterization

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Thus, the formed LAgNPs were characterized using surface plasmon resonance (SPR) pattern under UV–vis spectra ranging from 300 to 700 nm at different time points (0–30 min) using a Shimazu UV-2600 spectrophotometer. The average hydrodynamic diameter and stability of biogenic LAgNPs were determined using dynamic light scattering (DLS) and zeta potential studies by Microtrac's dynamic light scattering model Nanotrac. Shape, size, and elemental composition (energy-dispersive X-ray spectroscopy; EDS) were examined by transmission electron microscopy (TEM) using JEOL-2100, JEM USA. For TEM–EDS analysis, particles were coated on a carbon-coated 400 mesh copper grid. To analyze the involvement of various functional groups working as a surface-protecting agent on LAgNPs, Fourier-transform infrared spectroscopy (FTIR) analysis was carried out using Agilent Resolution Pro-carry 660 machine.
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5

Characterization of HDDA Nanoparticles for Drug Delivery

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The encapsulation ratio (ER) and loading coefficient (DL) of Apa or DOX in HDDA NBs were calculated via the equations shown below (1 and 2): ER(%)=WeightofApa/DOXloadedinHDDA/WeightofApa/DOXfedinitially×100% DL(%)=WeightofApa/DOXloadedinHDDA/WeightofHDDA×100% in which the weight of Apa or DOX loaded in HDDA was determined by UV−vis spectroscopy.
The morphology and size of HDDA and DDA were studied using a transmission electron microscope (JEM2100, JEOL Ltd., Japan). The zeta potentials and hydrodynamic sizes of HDDA and DDA were characterized by a zetasizer instrument (Nano ZS, Malvern Instruments, UK). The UV–vis absorption spectra of DOX, Apa, HA, Den, and HDDA solutions/suspensions were measured by a Shimadzu UV-2600 spectrophotometer (Japan).
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Purification and Characterization of Iron-Sulfur Cluster Protein HgcB

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HgcB was produced as a maltose-binding protein fusion construct (MBP-HgcB) and co-expressed with the pRKISC vector, which encodes an inducible copy of the E. coli isc operon involved in iron–sulfur cluster assembly17 (link). MBP-HgcB was lysed and purified under anoxic conditions (<1 ppm oxygen) using an amylose affinity resin. UV–visible spectra of MBP-HgcB were obtained with a Shimadzu UV-2600 spectrophotometer in a septum-sealed quartz cuvette, in a buffer containing 25 mM Na HEPES pH 7.5 and 2 mM dithiothreitol (DTT). The concentration of as-isolated (oxidized) [4Fe-4S] clusters was estimated using the molar extinction coefficient of 4 mM−1 Fe atoms at 390 nm43 (link).
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7

Comprehensive Characterization of Catalytic Materials

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The crystal phase formation of the as-prepared samples was determined using an X-ray diffractometer (XRD) (Bruker D8 Advance, Germany) with Cu Kα radiation (0.15406 nm, 40 kV, 40 mA). The morphologies of the samples were examined by scanning electron microscope (SEM) (Philips XL30 SFEG, the Netherlands) and HRTEM analyses (JEOL JEM-2100 Plus, Japan, operated at 200 kV). The elemental compositions of the samples were determined by energy-dispersive X-ray spectroscopy (EDS) analysis (Philips XL30 SFEG, Netherlands). Fourier transform infrared (FT-IR) analysis (Perkin Elmer Spectrum 100, Germany) was performed to determine the functional groups of the samples. The chemical states of the sample were identified using X-ray photoelectron spectrometer (XPS) analysis (Thermo Scientific Escalab 250Xi+, USA). N2 adsorption–desorption analysis, using the BELSORP model of Mini II (Japan), was used to explore the samples’ specific surface area and pore structure. The differential reflectance spectroscopy (DRS) of the samples was recorded using a Shimadzu UV-2600 spectrophotometer (Japan). The leaching concentrations of lanthanum, zinc, and iron ions were determined by ICP-MS using an Agilent 7800 (USA). To determine the by-products generated during the sonocatalytic degradation of metribuzin, GC–MS analysis was performed using an Agilent 6890 N (USA).
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8

Thermal and Spectroscopic Characterization of CMO Polymorph Mixture

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Temperature variable X-ray di raction of the CMO polymorph mixture was examined by X-ray the obtained CMO polymorph mixture and its temperature derivatives was studied using field emission scanning electron microscopy (Zeiss Ultra Plus, Germany) and high resolution transmission electron microscopy (JEOL Ltd. Tokyo Japan, JEM-2200FS). The thermal analysis was done using differential scanning calorimetric (DSC) measurement/thermogravimetric analysis (Netzsch 404 F3, Selb). The Raman spectra of the of the nominal CMO polymorph mixture and its temperature derivative compounds were recorded using a spectrometer (LabRam HR800, Horiba Jobin-Yvon, Villeneuve-88 nm Ar + laser. Fisher Scientific, ESCALAB -ray source was used for XPS analysis with the spectrometer calibrated with reference energies of Au 4f5/2 (83.9±0.1 eV) and Cu 2p3/2 (932.7±0.1 eV). A take-off angle of 90° was maintained between the surface and the analyser for the measurement. For the sample charging correction, the C 1s peak with a binding energy at 284.8 eV corresponding to the surface contamination was used for binding energy calibration. 42 The reflectance spectrum was recorded using a UV-Vis spectrophotometer (Shimadzu UV-2600 spectrophotometer) with a Shimadzu integrating sphere ISR-2600Plus (covering wavelength range 220-1400 nm).
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9

Quantification of Violacein Pigment in C. violaceum

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The culture of C. violaceum was grown in LB medium for 18 h in the absence and presence of varying concentrations of ZnO@Cs-NPs. To precipitate the insoluble pigment, 1.0 mL of overnight grown culture from each treatment group was centrifuged at 10,000 rpm for 5 min. Later, the pellet was re-suspended in 1.0 mL of DMSO and then vortexed vigorously for 30 sec. Following that, the solution was centrifuged again to remove the bacterial cell debris. The optical density (OD) of colored supernatant was recorded at 585 nm using UV-2600 Spectrophotometer, Shimadzu, Japan [50 (link)].
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10

Quantifying LDH Activity in Rat Colon Tissue

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The enzymatic activity of LDH was gauged by observing the change in absorbance at 340 nm via a spectrophotometer. This absorbance change occurs due to NADH oxidation in the following equilibrium reaction: pyruvate + NADH + H+ ←→ lactate + NAD+ [65 (link)]. The assay was initiated by incorporating Na-pyruvate (0.1 mL, 23 mmol/L) to a reaction mixture containing 2.9 mL phosphate buffer (0.1 mM), pH = 7.0; NADH (0.05 mL, 14 mmol/L, which was freshly prepared and maintained on ice to prevent the spontaneous oxidation of NADH); and sample (supernatant of rat colon tissue homogenate, 0.01 mL). The definition of one unit of LDH activity (U) was the enzyme’s ability to convert 1 μmol of NADH each minute under the assay conditions. The total LDH activity, reflected by the reduction in absorbance, was quantified using a UV-2600 spectrophotometer (Shimadzu, Kyoto, Japan).
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