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19 protocols using v 750 uv vis spectrophotometer

1

Photocatalytic Reduction of Cr(VI) and Phenol

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For the reduction of Cr(VI), the aqueous
solution of K2Cr2O7 was used. A 20
mL volume of 100 ppm hexavalent Cr solution was taken with 0.02 g
of catalysts to test the photocatalytic activity. To check the effect
of pH on the photocatalytic reduction process, the pH of the solution
was maintained at 2, 4, 6, and 8. Then, the suspension was stirred
under dark condition for 30 min to attain the adsorption and desorption
equilibrium before irradiation under solar light (100 000 lx).
At different time intervals, the catalysts were separated by centrifugation
and the supernatant was used for colorimetric analysis at 540 nm by
1,5-diphenylcarbazide (DPC) method using a JASCO V-750 UV−Vis
spectrophotometer.14 (link) Additionally, the
remained Cr in the sample after the experiment was also determined.15 (link)Photocatalytic degradation of phenol was
carried out by taking 20 mg of catalyst with 20 mL of 10 ppm phenol.
Then, the suspension was stirred under dark condition for 30 min to
attain the adsorption and desorption equilibrium before irradiation
of solar light. Then, the pH of phenol solution was maintained at
2, 4, 6, and 8. After the photocatalytic experiment, the catalyst
was extracted from the phenol solution by centrifugation and the residue
was directly analyzed by a JASCO V-750 UV−Vis spectrophotometer.
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2

Covalent Serine Binding to Tryptophan Synthase

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Absorbance titration experiments of covalent serine binding to TS were performed in a 1 cm quartz cuvette and an UV/Vis photometer (Jasco V750-UV/Vis spectrophotometer, Jasco Deutschland, Pfungstadt, Germany). Reduction of the internal aldimine peak signal at 412 nm was followed as a function of serine concentration. For this the spectra (350–700 nm) of 30 µM TS (1:1 TrpA:TrpB) in 50 mM, Tris·HCl pH 7.5, and alternatively 100 mM CsCl, were recorded after each step-wise addition of serine (0.001–15 mM end concentrations) and incubated at room temperature for 3 min. The internal aldimine peaks were isolated by linear baseline correction at wavelengths 380 nm and 450 nm, and the derived absorbance at 412 nm was subtracted from the initial absorbance at 0 mM serine. The resulting data were plotted against the serine concentration and fitted with equation (3) in Origin 2018 (OriginLab, Northampton, MA, USA) to obtain the apparent Kd,app value of covalent serine binding.
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3

Thermal Difference Spectroscopy of Oligonucleotides

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UV samples of investigated oligonucleotides were prepared using a buffer solution: KH2PO4/K2HPO4 (1 mM, pH 7.0), KCl (5 mM). For each oligonucleotide sample, a UV spectrum was recorded above and below its melting temperature (Tm). All experiments were performed on a Jasco V 750 UV/Vis spectrophotometer (Jasco, Tokyo, Japan) using quartz cuvettes with an optical path of 1 cm and at 25 μM strand concentration. Absorbance spectra were recorded in the 220–340 nm range, with a scan speed of 200 nm min−1 and a data interval of 1 nm. The difference between the UV spectra at high (95 °C) and low (20 °C) temperatures was defined as the TDS; this represents the spectral difference between the unfolded and folded forms. The temperature (20 or 95 °C) was kept constant with a thermostatic circulating water bath for cell holders (Jasco CTU-100). The thermal difference spectra were normalized (+1 for the highest positive peak).
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4

Comprehensive Material Characterization Protocol

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The phase purity of the as-prepared materials were characterized by XRD, Rigaku Miniflex powder diffractometer) with Cu Kα as radiation source (λ = 1.54 Å, 30 kV, 50 mA). The functional groups associated with the bending and stretching mode of vibration of the materials were specified by JASCO FT-IR-4600, using KBr reference. The exterior surface morphology and structural features of the materials were obtained by FESEM by using ZEISS Sigma 500 VP microscope. The internal structure and morphology of the material was explored under the TEM and HR-TEM analysis by using JEOL 2100. The XPS measurement was taken at an X-ray photoelectron spectrometer (ESCALAB 250XI) with X-ray source as nonmonochromatized Mg Kα and energy of 0.8 eV. The optical absorption measurements were recorded by JASCO-V-750 UV–Vis spectrophotometer. The PL emission spectra were recorded by applying excitation energy of 320 nm using JASCO-FP-8300 spectrophotometer. The surface area of the MgCr-LDH based samples were measured by N2 adsorption–desorption Brunauere–Emmett–Teller (BET) measurements using NOVA Quantachrome TouchWin v1 0.22. The pore size distribution and pore volume were obtained by applying the BJH model. PEC measurements of samples were carried out by potentiostat–galvanostat (IviumStat) terminal.
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5

Quantification of Aniline Tetramer on Dragline Silk

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UV-Vis analysis of the aniline tetramer was performed with JASCO V-750 UV-Vis spectrophotometer (JASCO International Co. Ltd., Tokyo, Japan). The as-synthesized emeraldine base (EB) state of aniline tetramer was dissolved in N-methyl-2-pyrrolidone for measurement at room temperature. In addition, UV-Vis spectroscopy was also utilized to quantitatively determine the amount of aniline tetramer modified on the surface of dragline silk. Firstly, the specific amount of electroactive fiber was immersed in 95% ethyl alcohol with assisted with sonication to strip off all the aniline tetramer attached on the surface of the dragline silk. Subsequently, the resulting aniline tetramer solution was analysed with UV-Vis spectroscopy by measuring the absorbance at 588 nm wavelength and the aniline tetramer concentration could be calculated according to the calibration curve (eqn (2) in Fig. S1). Therefore, the amount of aniline tetramer on the silk surface could be obtained.
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6

Protein Adsorption Measurement Protocol

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The protein adsorption studies were performed with ALB concentration in the range of 0.1–2.6 mg/mL. The mixtures were shaken at 120 rpm in a thermostated shaker for 2 h at 310 K. The protein concentration in obtained supernatants was measured using a Jasco V-750 UV-Vis spectrophotometer (Jasco Corporation, Tokyo, Japan) in a wavelength range of 200–450 nm (the area of the 280 nm band).
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7

Comprehensive Characterization of Materials

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Transmission electron microscopy (TEM) was performed on JEOL JEM-2010 high resolution transmission electron microscope operated at 200 kV. X-ray photoelectron spectroscopy (XPS) was performed on an Thermo Fisher Scientific K-Alpha X-ray photoelectron spectrometer. FTIR spectrum was collected at room temperature (on a Jasco FTIR-4100 spectrometer) from sample prepared as pellets with KBr. The UV–Vis absorption spectrum was recorded with V-750 UV–Vis spectrophotometer (Jasco). Steady-state and time-resolved PL measurements were performed based on a spectrophotometers (Fluotime 300, PicoQuant). A pulsed Xenon lamp was used as an excitation source and the PL emission excited at ~400 nm is collected by a PMT detector with the calibration according to the wavelength-response function of our detector. The instrument response function for our whole time-resolved PL measurement system is ~400 ns. Absolute PL-QY measurement was performed based on the aforementioned spectrometer incorporated with an integrating sphere. The excitation and emission spectra were measured for both reference and experimental samples by the calibrated detectors. In this case, the ratio between total amounts of photons emitted and absorbed can be determined, thus the PL-QY can be deduced.
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8

Inertness Study of Mn(II) Complexes

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The inertness of the [Mn(tO2DO2A)] and [Mn(tO2DO2APip)]2+ complexes was studied by metal exchange reactions using Cu(II) ion as ligand scavenger in 10–40-fold excess relative to the complex concentration (ccomplex = 0.4 mM). The reactions were monitored by a JASCO V750 UV-Vis spectrophotometer (Waltham, MA, USA) (25 °C (Peltier thermostated), I = 0.15 M NaCl, 1 cm micro quartz cuvette—Vtot = 500 μL). The kinetic studies were carried out in N,N′-dimethylpiperazine buffer to maintain the pH constant in the range 3.4–5.0 (cDMP = 50 mM, log K2H = 4.19). The rate constants (kobs) of the reactions were calculated by fitting the absorbance-time data pairs to the Equation (9).
At = A0Atekobst+Ae,
where At, A0 and Ae are the absorbance at time t, at the start and at equilibrium, respectively. The high excess of the Cu(II) ion ensures the pseudo-first-order condition for the reactions, thus the reaction rate can be given by Equation (10) and kobs can be handled as pseudo-first-order rate constant.
dMnLtdt = kobsMnLt.
The calculations were performed with the computer program Micromath Scientist, version 2.0 (Salt Lake City, UT, USA) by using a standard least-squares procedure.
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9

Encapsulation Efficiency of Betamethasone Nanoparticles

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NG EE was measured using the indirect method based on quantification of unloaded free drug [21 (link)]. BR Ext-loaded NGs were centrifuged at the speed of 5500 rfc (GyroSpin centrifuge, LabTech®, Sorisole, Italy) for 10 min. The BR Ext in the supernatant (free BR Ext) was measured at 538 nm (Bet maximum absorption lambda) by employing a Jasco V-750 UV-Vis Spectrophotometer (Tokyo, Japan). This Bet in the BR Ext amount was subtracted from the initial one (total amount of Bet) for the encapsulation calculation. The pertinent calibration curve was constructed and the %EE was determined via the following equation [22 (link)]: EE (%)=[Total amount of BetFree BetTotal amount of Bet ]×100
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10

Spectroscopic Analysis of Protein Structure

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UV−vis absorption spectra were recorded at 25°C using a 1.0 cm optical path-length quartz cells on a JASCO V-750 UV−vis spectrophotometer in the range of 240–700 nm, using protein concentration of 0.25 mg/mL in 20 mM Tris-HCl buffer pH 7.4. Other experimental parameters were bandwidth 2.0 nm, scanning speed 200 nm/min, data pitch 1.0 nm.
Far UV-CD spectra were recorded on a Jasco J-715 spectropolarimeter equipped with a Peltier thermostatic cell holder using a 0.1 cm path length quartz cell. Spectra were registered at 25°C in the range of 190–250 nm at a protein concentration of 0.05 mg/mL in 20 mM Tris-HCl buffer pH 7.4. Measurements were recorded with a time constant of 2 s, a 2 nm bandwidth, and a scan rate of 50 nm/min. Three scans for each spectrum were acquired.
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