The designed potentiometric system included a manufactured standard tramadol hydrochloride-phosphomolybdate (TRD-PM) or functionalized TRD-PM-CeO2/Al2O3 nanocomposite coated wire sensor, as well as a reference silver/silver chloride (Ag/AgCl) sensor (JEOL Ltd., Tokyo, Japan). Furthermore, the presence of Ce, Al, and O elements in the synthesized nanomaterials was detected using Energy-Dispersive X-ray Spectroscopy (EDX) analysis combined with EDX-8100 (Shimadzu, Kyoto, Japan). Different spectroscopic and microscopic methods were applied to characterize the synthesized metal oxide nanoparticles and nanocomposite, including UV-2450 spectrophotometer (Shimadzu Corporation, Kyoto, Japan), the Fourier-Transform Infrared spectroscopy (FT-IR) Spectrum BX spectrometer (Shimadzu Corporation, Kyoto, Japan), and the UV-2450 spectrophotometer (Shimadzu Corporation, Kyoto, Japan (PerkinElmer, Waltham, Massachusetts, United States). Shimadzu XRD-6000 diffractometer (Shimadzu, Kyoto, Japan), JSM-7610F scanning, and transmission electron microscopes (SEM-JEOL and TEM-JEM-2100F Ltd., Tokyo, Japan) were used for microscopic investigations. Furthermore, Energy-Dispersive X-ray Spectroscopy (EDX) analysis utilizing the (EDX-8100, Shimadzu, Kyoto, Japan) was utilized for elemental analysis.
Uv 2450 spectrophotometer
Manufactured by Shimadzu
Sourced in Japan, China
The UV-2450 is a double-beam spectrophotometer designed for accurate and reliable UV-Visible absorption measurements. It features a wavelength range of 190 to 1100 nm and a spectral bandwidth of 1.0 nm. The UV-2450 provides high-resolution data collection and advanced data processing capabilities.
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Lab products found in correlation
Silica gel, by Qingdao Haiyang Chemical (13 mentions)
Escalab 250xi, by Thermo Fisher Scientific (4 mentions)
Vertex 70 spectrometer, by Bruker (4 mentions)
Ultra plus, by Zeiss (4 mentions)
Tcc 240a, by Shimadzu (4 mentions)
Ir prestige 21 spectrometer, by Shimadzu (4 mentions)
Fluorolog 3 tcspc spectrofluorometer, by Horiba (4 mentions)
Nicolet 6700 ft ir spectrometer, by Thermo Fisher Scientific (4 mentions)
P 1020 polarimeter, by Jasco (4 mentions)
Tensor 37 infrared spectrophotometer, by Bruker (3 mentions)
Esi interface, by Shimadzu (3 mentions)
Mercury 400 nmr spectrometer, by Agilent Technologies (3 mentions)
Micromass q tof mass spectrometer, by Waters Corporation (3 mentions)
Jsm 7600f microscope, by JEOL (3 mentions)
Suc aapf pna, by Merck Group (3 mentions)
Cary eclipse fluorescence spectrophotometer, by Agilent Technologies (3 mentions)
Rf 5301pc spectrofluorometer, by Shimadzu (3 mentions)
Tensor 27 spectrometer, by Bruker (3 mentions)
Jem 2100, by JEOL (3 mentions)
Gf254 glass plates, by Qingdao Haiyang Chemical (3 mentions)
296 protocols using uv 2450 spectrophotometer
1
Potentiometric Sensor for Tramadol Detection
2
Opn5m Mutant Protein Transient Absorption
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UV/Vis absorption spectra were recorded using a Shimadzu UV2400 or UV2450 spectrophotometer and an optical cell (width, 2 mm; light path, 1 cm). The sample temperature was maintained by a temperature controller (RTE-210, NESLAB) at 0 ± 0.1 °C. The sample was irradiated with light which was generated by a 1-kW tungsten halogen lamp (Master HILUX-HR, Rikagaku Seiki) and passed through optical filters (Y-52 or UV-D36C, AGC Techno Glass). The transient absorption spectra of Opn5m T188C mutant protein were recorded using a Shimadzu UV2450 spectrophotometer at 10 ± 0.1 °C. The spectra were measured in the dark and after 2 min irradiation with light which was generated by a 1-kW tungsten halogen lamp and passed through an optical filter (Y-52, AGC Techno Glass). The transient absorption spectra of Opn5m T188C mutant protein were also recorded using a high-speed CCD camera spectrophotometer (C10000 system, Hamamatsu Photonics) kept at 37 ± 0.1 °C by a temperature controller (qpod, QUANTUM Northwest)25 (link) to accelerate the photocyclic reaction, according to the methods used in our previous study for Opn5L118 (link). The flash light for irradiation was generated by a short-arc power flash (SA-200, Nissin Electronic; pulse duration of ~170 μs and flash lamp input of 200 J/F) and passed through an optical filter (Y-48, AGC Techno Glass).
3
Bacterial Culture Preparation and Quantification
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Microbiological experiments were conducted with Gram-negative Escherichia coli (E. coli ATCC 25922) and Gram-positive Staphylococcus aureus (S. aureus ATCC 25923). Bacteria were stored at -80°C in culture media-glycerol aliquots. Before the experiments, they were incubated overnight at 30°C on Lysogeny Broth (Miller-LB, 20 g.L -1 ) agar (15g.L -1 ) plate for E. coli and at 37°C on Mueller-Hinton (MH, 25g.L -1 ) agar (15g.L -1 ) plate for S. aureus.
Then, a liquid pre-culture was prepared with one colony of E. coli or S. aureus in LB or MH media, respectively, and stirred overnight (90 rpm) at 30°C or 37°C. Bacterial concentration in liquid culture was estimated via UV-Vis spectroscopy (UV-2450 Shimadzu spectrophotometer) at 620 nm using a calibration curve. At this stage, the initial bacterial concentration is close to 10 9 CFU.mL -1 .
Then, a liquid pre-culture was prepared with one colony of E. coli or S. aureus in LB or MH media, respectively, and stirred overnight (90 rpm) at 30°C or 37°C. Bacterial concentration in liquid culture was estimated via UV-Vis spectroscopy (UV-2450 Shimadzu spectrophotometer) at 620 nm using a calibration curve. At this stage, the initial bacterial concentration is close to 10 9 CFU.mL -1 .
4
Electrochemical Deposition of Microtubes
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Template electrochemical deposition of multi-layer microtubes was carried out with a CHI 661D potentiostat (CH Instruments, Austin, TX). Scanning electron microscopy (SEM) images were obtained with a Phillips XL30 ESEM instrument, using an acceleration voltage of 20 kV. Energy-dispersive X-ray mapping analysis was performed using an Oxford EDX detector attached to SEM instrument and operated by INCA software. An inverted optical microscope (Nikon Instrument Inc. Ti-S/L100), coupled with a 20× and 40× objectives, a Photometrics QuantEM 512/SC camera (Roper Scientific, Duluth, GA) and MetaMorph 7.6 software (Molecular Devices, Sunnyvale, CA) were used for capturing movies at a frame rate of 30 frames per sec. The speed of the micromotors was tracked using a Metamorph tracking module and the results were statistically analyzed using Origin software.
The absorbance was measured between 500 and 800 nm using a UV-2450 Shimadzu spectrophotometer.
The absorbance was measured between 500 and 800 nm using a UV-2450 Shimadzu spectrophotometer.
5
Enzymatic Activities for NAD+ Synthesis
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Enzyme activities were determined as previously described [18 (link)]. Briefly, substrate was continuously converted to NADH through a coupled reaction at 60 °C, and NADH concentration was measured by absorbance changes at 340 nm using a UV-2450 spectrophotometer (Shimazu, Japan) (Additional file 1 : Figure S2). The standard mixture was composed of 400 mM HEPES–NaOH (pH 8), 60 mM NH4Cl, 10 mM MgCl2, 1 mM polyphosphate (Cat: 28-2880-5; Sigma, Germany), 0.2 mM ATP, 1 mM glucose and an excess amount of glucose dehydrogenase (GDH). A moderate amount of the enzyme of interest and an excess of enzymes catalyzing downstream reactions of NAD+ salvage synthesis was added to the standard mixture, so that NADH production rate reflected the activity of the enzyme of interest. Substrates were used at the final concentration of 0.2 mM for determining enzyme activity as follows; deamino-NAD+ (NaAD) for NADS, nicotinate mononucleotide (NaMN) for NaMAT, nicotinate (NA) and phosphoribosyl pyrophosphate (PRPP) for NaPRT, NA and ribose-5-phosphate (R5P) for RPK, NA and ADP-ribose for ADPRP, and NAM and PRPP for NAMase, respectively. The overall performance of the integrated strain was assessed using NAM and ADP-ribose as substrates. Reaction mixtures were incubated at 60 °C for 1 min prior to substrate addition.
6
Comprehensive Nanomaterial Characterization Protocol
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SEM was carried out on the ZEISS SUPRA 55 (Carl Zeiss, Germany) field‐emission scanning electron microscope and the EDS data were acquired at an accelerating voltage of 5.0 kV. TEM and high‐resolution transmission electron microscopy (HR‐TEM) were performed on the FEI Tecnai G2 F30 transmission electron microscope at an acceleration voltage of 200 kV. AFM was conducted on the drop‐cast flakes on the SiO2 substrate using the Bruker Dimension Icon atomic force microscope (Bruker, USA). Fourier‐transfer infrared (FTIR) spectroscopy was carried out on the PerkinElmer Frontier with the ATR accessory and XPS was performed on the Thermo Fisher ESCALAB 250Xi. The absorption spectra were obtained on the Lambda25 UV–vis–NIR spectrophotometer and DRS data were acquired on the Shimazu UV‐2450 spectrophotometer. Raman scattering was conducted on the Horiba Jobin Yvon LabRam HR‐VIS high‐resolution confocal Raman microscope equipped with a 633 nm laser. The DSC curves were obtained on the TA Instruments Q20 differential scanning calorimeter at a scanning rate of 5 °C min−1 from 0 to 60 °C under nitrogen at a flow rate of 50 mL min−1. To evaluate the photothermal properties, the temperature change was monitored by an infrared thermal imaging camera (Fluke Ti27, USA).
7
Aptamer Thermal Stability Analysis
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UV absorbance versus temperature profiles (melting curves) was measured for each aptamer at two wavelengths, 260 and 295 nm, by TMSPC-8 with a SHIMAZU UV-2450 spectrophotometer. ODNs were prepared at 4 μM in phosphate buffer containing NaCl (10 mM Na2HPO4, 10 mM NaH2PO4, and 100 mM NaCl [pH 7.4]) or phosphate buffer containing KCl (10 mM Na2HPO4, 10 mM NaH2PO4, and 100 mM KCl [pH 7.4]). These samples were then heat annealed to 90°C and allowed to slowly cool to 4°C over a period of several hours. Then 110 μL of a sample was transferred to a 1-cm path-length quartz cuvette and covered with a layer of 30 μL liquid paraffin. It was heated to 95°C and cooled to room temperature at 0.5°C/min, with data collection occurring every 0.5 min on the annealing and melting steps.
8
Spectrophotometric Determination of Protein
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To determine total water soluble protein content, the supernatant from the air-brushed tissue was used. The supernatant was analyzed in a SHIMADZU UV 2450 spectrophotometer (Shimadzu, Kyoto, Japan) recording absorbance values at 235 and 280 nm. Total water soluble protein content was determined using the equations of [94 (link)].
9
Biophysical Characterization of Biomolecules
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All the absorbance measurements were carried out on SHIMADZU UV-2450 spectrophotometer (Shimadzu, Japan). Fluorescence measurements were performed on HITACHI FL-4600 fluorescence spectrophotometer (Hitachi, Japan). Circular dichroism measurements were measured on J-810 CD spectrometer (Jasco, Japan). Calorimetric experiments were carried out on MicroCal ITC200 isothermal titration microcalorimeter with a workstation. ROS measurements were evaluated on a FACS AriaIII flow cytometry (BD, US).
10
Stoichiometric Analysis of DpdtpA-Copper Interaction
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The stoichiometry of the reaction between DpdtpA and copper chloride was determined as previously described [25 (link)]. Briefly, solutions of 1 mM DpdtpA in 50% DMSO and 1 mM CuCl2 in water were prepared. Next, 0.04 mL of the CuCl2 solution was added to a series of 5 mL-volumetric flasks, and then a different volume of DpdtpA (10, 20, 30, 40, 50, 60, 70, 80, 85, and 90 µL) was added to each flask. Finally, 50 mM Tris-HCl buffer (pH 7.4) was added to total 5 mL. After mixing and equilibrium, the UV spectra were recorded on a Shimadzu-UV-2450 spectrophotometer (Shimadzu Co., Ltd., Suzhou, China).
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