Estimated oil equivalents were measured every 24 h according to the method of Wade et al. (50 ) from a spigot 10 cm above the bottom of each tank. Briefly, the fluorescence of dichloromethane extracts (5 to 10 ml) was measured at 260/358-nm excitation/emission, respectively, using a spectrofluorometer (Shimadzu RF-5300). The florescent response was compared to a five-point calibration curve prepared using Macondo surrogate oil.
Rf 5300
Manufactured by Shimadzu
Sourced in Japan
The RF-5300 is a fluorescence spectrophotometer manufactured by Shimadzu Corporation. It is designed to measure the fluorescence properties of samples. The core function of the RF-5300 is to excite samples with light and detect the resulting fluorescence emission.
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9 protocols using rf 5300
1
Measuring Oil Equivalents in Aquatic Tanks
2
Characterization of Chemical Compounds
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1H and 13CNMR spectra were recorded with a Bruker Ascend 400 spectrometer (Parque Tecnológico de AndalucíaC/Severo Ochoa, Málaga, Spain, 400 MHz for 1H and 100 MHz for 13C) using TMS (δ = 0 ppm) as an internal standard for 1H NMR and CDCl3 (δ = 77 ppm) or DMSO-d6 (δ = 39.7 ppm) as that for 13C NMR spectroscopy (Parque Tecnológico de AndalucíaC/Severo Ochoa, Málaga, Spain). High-resolution mass spectra (FAB) were recorded by using a JEOL JMS-700 instrument (Musashino Akishima, Tokyo, Japan)with m-nitrobenzyl alcohol as the matrix and PEG-200 as the calibration standard. UV-vis spectra were recorded on a Shimadzu UV-2600 spectrometer in the wavelength range of 200–600 nm (Tokyo, Japan). Fluorescence emission spectra were recorded on a Shimadzu RF-5300 in the wavelength range of 300–600 nm (Tokyo, Japan). Excitation and emission wavelengths were, respectively, 300 and 390 nm or 360 and 430 nm. All fluorescence emission spectra were recorded bandwidths of 1.5 nm for excitation and 1.5 nm for emission. HPLC analysis was performed on a Shimadzu LC system (Tokyo, Japan, pump: LC-20AD, column oven: CTO-20A, UV detector: SPD-20AV at 370 nm, and degasser: DGU-20A3) with a Shimadzu VP-ODS column. The mobile phase was MeOH/H2O (2/3 v/v), the flow rate was 0.75 mL/min, and the column temperature was kept at 40 °C.
3
HPLC Analysis of Compounds
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The HPLC system consisted of a Shimadzu LC-10 AD pump (Kyoto, Japan) equipped with a Shimadzu RF-5300 fluorescence detector and a Shimadzu CTO-6A column oven. The analytical column was a reverse-phase Hydrosphere C18 column (internal diameter [i.d.], 4.6 × 50 mm, 5 μm), which was purchased from YMC Co., Ltd. (Kyoto, Japan).
4
Protein Fluorescence Emission Analysis
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The intrinsic fluorescence emission spectra of proteins were analyzed by a fluorescence spectrophotometer (RF-5300, Shimadzu, Japan) at 25 °C [14 (link)]. The protein sample solution (0.2 mg/mL) was prepared with phosphate buffer (10 mM, pH 7.0), where the phosphate buffer was set as blank. The optical length of the quartz cuvette, excitation wavelength, scan range of emission wavelength, and slit width was 1 cm, 290 nm, 300–400 nm, and 3 nm, respectively.
5
Determination of Protein H0 via ANS Fluorescence
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H0 determination was carried out in accordance with the procedure of Sheng et al. [16 (link)]. The protein sample solution was diluted to different concentrations (0.20, 0.40, 0.60, 0.80, and 1.0 mg/mL) with phosphate buffer (10 mM, pH 7.0). Then 10 μL of ANS (8 mM, pH 7.0) was added to 2 mL of each diluted sample solution, mixed thoroughly with a vortex shaker, and placed in the dark for 15 min. The fluorescence intensity was measured using a spectrofluorophotometer (RF–5300, Shimadzu, Japan) at an emission wavelength of 470 nm and an excitation wavelength of 390 nm. When plotting the figure of fluorescence intensity vs. the concentration of the protein, the slope was defined as the H0 of the protein.
6
Fluorescence Spectroscopy Measurements
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The fluorescence parameters including fluorescence excitation/emission wavelength and intensity were measured by an RF-5300 and RF-1500 fluorescence spectrophotometer (Shimadzu).
7
Chlorophyll Content Determination in Seedlings
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The shoot of the 14-day-old seedling was cut at the hypocotyl and weighed to determine FW. Then, the shoot was incubated in 80% (v/v) acetone at 4 °C in darkness for two days to extract lipophilic pigments. The absorbance of the acetone extract at 720, 663.2, and 646.8 nm was measured with a spectrometer (V-730 BIO, JASCO, Tokyo, Japan) to determine the total content (Chl a + Chl b) as described [43 (link)]. For pgp1-2, sqd1 pgp1-2, and sqd2-2 pgp1-2, the Chl content in a seedling was below a detection limit in the spectrometric analysis. Therefore, for these mutants, intensity of Chl fluorescence at 666 nm under 435 nm excitation was measured with a fluorospectrometer (RF5300, Shimadzu, Kyoto, Japan) and total Chl content was determined by using a known concentration of Chl as a standard.
8
Protein Fluorescence Analysis under pH Conditions
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Fluorescence spectra were scanned using a fluorescence spectrophotometer (RF-5300, Shimadzu Co., Kyoto, Japan), where the excitation wavelengths were set at 295 nm, and the emission wavelength range was set at 300–450 nm. The excitation slit width and emission slit width were both 10 nm [34 (link)]. The changes of fluorescence intensity of three protein solutions (0.5 mg/mL) before and after heated at 70 °C for 30 min with pH 5.0, 7.0 and 9.0 were recorded.
9
Caspase Activation Assay Protocol
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Caspase activation was measured using a caspase fluorometric substrates; Ac-Leu-Glu-His-Asp-MCA for caspase-9 substrate peptide and Ac-Asp-Asn-Leu-Asp-MCA for caspase-3 substrate peptide (PEPTIDE institute, Osaka, Japan). Cells were incubated in a presence and absence of E2 for 12 h. Protein (50 µg) was mixed with PBS and substrate peptide (10 µM) followed by incubating 37˚C for 2 h. After that, the fluorescent signals were measured using a spectrofluorometer (RF-5300) (Shimadzu, Kyoto, Japan) with excitation at 380 nm and emission at 460 nm.
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