F 4500 fluorometer

Manufactured by Hitachi

Sourced in Japan

The F-4500 fluorometer is a compact, high-performance instrument designed for accurate fluorescence measurements. It features a high-intensity xenon lamp, a monochromator-based excitation and emission system, and a photomultiplier tube detector. The F-4500 fluorometer is capable of wavelength scanning, time-based analysis, and various other fluorescence-based techniques.

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Lab products found in correlation

Uv vis spectrophotometer, by Hitachi (1 mentions) Dh mini light source, by OceanOptics (1 mentions) Infinite m200 pro plate reader, by Tecan (1 mentions) V 650, by Jasco (1 mentions) Quartz glass cuvette, by Hellma (1 mentions) Advance 500 mhz spectrometer, by Bruker (1 mentions) Evolution 201 spectrophotometer, by Thermo Fisher Scientific (1 mentions) Jem 2100, by JEOL (1 mentions)

13 protocols using f 4500 fluorometer

Luminescence Lifetime of 1c Solution

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The luminescence lifetime of a 1 mM solution of 1c was measured in H₂O and D₂O on a Hitachi (San Francisco, CA) F4500 fluorometer, using a λ_ex = 232 nm and λ_em = 544 nm. Twenty-five scans were acquired, averaged, and fit to a monoexponential decay function.

MacRenaris K.W., Ma Z., Krueger R.L., Carney C.E, & Meade T.J. (2016). Cell-Permeable Esterase-Activated Ca(II)-Sensitive MRI Contrast Agent. Bioconjugate chemistry, 27(2), 465-473.

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Photochemical Uncaging Characterization

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Absorption and fluorescence spectra were recorded in quartz glass cuvettes with either 10 mm or 2 mm optical path length (Hellma Analytics) on a Jasco V‐650 UV‐vis spectrophotometer and a Hitachi F‐4500 fluorometer. Absorption spectra were measured at an optical density (OD) close to 1. OD values for fluorescence spectra measurements were set to 0.1 to 0.15. Data for ON1 was obtained on a Tecan Infinite M200 Pro plate reader.
Uncaging quantum yields were determined using our recently published fulgide actinometry setup controlled by our in‐house programmed software PHITS (Photoswitch Irradiation Test Suite) written with LabVIEW.^[43] A concentrated indolylfulgide photoswitch solution in toluene served as a reference for the chemical actinometry. Its absorption spectrum was tracked (Ocean Optics DH‐mini light source, Ocean Optics USB4000 or Thorlabs CCS200/M detector) while converting the fulgide from its closed form to the Z‐form through irradiation with a 530 nm LED (M530 L3, Thorlabs). The caged oligonucleotide was then irradiated in the same setup with known photon flux. Last, the photolysis rate was determined by integration of the RP‐HPLC signals.

Kaufmann J., Müller P., Andreadou E, & Heckel A. (2022). Green‐Light Activatable BODIPY and Coumarin 5’‐Caps for Oligonucleotide Photocaging. Chemistry (Weinheim an Der Bergstrasse, Germany), 28(36), e202200477.

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Determining Lanthanide Coordination in Complexes

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The number of water molecules directly coordinated to the lanthanide center (q), was determined for each of the Tb^III analogues 5a’-c’ (See Table S2), 10a’-d’ (Table 1), and 11’ in MilliQ water and MOPS/carbonate buffer (10 mM MOPS, 24 mM NaHCO₃, pH 7.4). The monoexponential fluorescence decay of an ~ 1 mM solution of each complex was determined using a Hitachi F4500 fluorometer (Schaumburg, IL). An excitation wavelength of 395 nm and an emission wavelength of 614 nm were used, and 25 scans were acquired and averaged for each solution. The averaged data was fit with a monoexponential decay function, and the time constant (τ) for each solution was determined in triplicate. The fluorescence decay curves of the complexes were measured in both H₂O and D₂O, and in both buffer and deuterated buffer - obtained by lyophilizing and re-suspending the buffer in D₂O three times (Figure S8). The q values were calculated using the empirically derived Horrock’s equation for Tb^III (Eq. 2):^{[17 (link)]}

q = 4.2 (\frac{1}{τ_{H}} - \frac{1}{τ_{D}} - 0.06)

Lilley L.M., Kamper S., Caldwell M., Chia Z.K., Ballweg D., Vistain L., Krimmel J., Mills T.A., MacRenaris K., Lee P., Waters E.A, & Meade T.J. (2019). Self-Immolative Activation of β–galactosidase Responsive Probes for In Vivo MR Imaging in Mouse Models. Angewandte Chemie (International ed. in English), 59(1), 388-394.

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Efflux Assay for Antibiotic Resistance

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For this test, a modification of the procedure described by Kaatz et al. (2000) and Patel et al. (2010) was used. Cells were grown overnight in suitable broth and adjusted to 0.4 McFarland. Ten μg/mL of EB (final concentration) was added and incubated for 25 min at room temperature. Cells were harvested by centrifugation (7000 ×g) and washed with fresh culture media, and then 4 mL of suitable broth was added. The suspension was maintained at 30°C or 37°C, and the fluorescence of aliquots was determined at frequent intervals of time (5–30 min) in a Hitachi F‐4500 fluorometer, Tokyo (excitation wavelength, 540 nm; emission wavelength 545 nm).
Expression of efflux with significant differences was in accordance with that described by Patel et al. (2010) where at least a 20% difference of the fluorescence intensity has to be achieved between the tested strains and the control.

Wacher‐Rodarte M.D., Trejo‐Muñúzuri T.P., Montiel‐Aguirre J.F., Drago‐Serrano M.E., Gutiérrez‐Lucas R.L., Castañeda‐Sánchez J.I, & Sainz‐Espuñes T. (2015). Antibiotic resistance and multidrug‐resistant efflux pumps expression in lactic acid bacteria isolated from pozol, a nonalcoholic Mayan maize fermented beverage. Food Science & Nutrition, 4(3), 423-430.

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Protein Aromatic Amino Acid Analysis

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The protein samples were dissolved in 0.01 M PBS (pH 7.0) to obtain the final concentration of 1 mg/mL. Then, the changes in the protein aromatic amino acid residues were determined using a Hitachi F4500 fluorometer (Tokyo, Japan) with an excitation wavelength of 298 nm and a scanning wavelength of 323~450 nm.

Wu S.S., Han W., Cheng Y.F., Yun S.J., Chang M.C., Cheng F.E., Cao J.L, & Feng C.P. (2023). Transglutaminase-Catalyzed Glycosylation Improved Physicochemical and Functional Properties of Lentinus edodes Protein Fraction. Foods, 12(9), 1849.

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DNA Fluorescence Titration with Mesoionic Compounds

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Fluorescence emission spectroscopic titration experiments of DNA were conducted in the absence and presence of a constant concentration of the mesoionic compounds 5a–d. The assay was performed using 2 and 10 ng/mL of salmon DNA (Sigma-Aldrich/Merck) at 37 °C. After that, the fluorescence emission was recorded after 1 h of DNA incubation with or without compounds 5a–d (25 µM) or DMSO, over a wavelength range of 300 to 600 nm in a Tris-acetate-EDTA buffer (Promega) at room temperature. The slit widths for excitation and emission were set to 5.0 nm. The fluorescence was examined using a F4500 fluorometer (Hitachi, New Jersey, NJ, USA).

Sousa-Pereira D., Silva de Oliveira T., Paiva R.O., Chaves O.A., Netto-Ferreira J.C., Echevarria-Lima J, & Echevarria A. (2020). Synthetic (E)-3-Phenyl-5-(phenylamino)-2-styryl-1,3,4-thiadiazol-3-ium Chloride Derivatives as Promising Chemotherapy Agents on Cell Lines Infected with HTLV-1. Molecules, 25(11), 2537.

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Determination of Peanut Protein's H0

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H₀ was determined by a modified method of Huang et al. [40 (link)]. 0.01 M phosphate buffer (pH 7.0) was used to dissolve peanut protein. The solution was magnetically stirred for 1 hour and then centrifuged at 10,000 rpm for 10 min. After that, the up-layer solution was collected and its concentration was detected with the Biuret method [41 ]. The concentration of protein was then diluted to 0.05–0.5 mg/mL with the same phosphate buffer. To 4 mL of different concentration samples 40 μL of 8 mM ANS were added. The detection of fluorescence intensity was carried out at excitation wavelength 390 nm and emission wavelength 470 nm with an F-4500 fluorometer (Hitachi, Tokyo, Japan). The fluorescence intensity was plotted against the protein concentration, and the slope of the curve was the H₀ of peanut protein.

Sun X., Jin H., Li Y., Feng H., Liu C, & Xu J. (2018). The Molecular Properties of Peanut Protein: Impact of Temperature, Relative Humidity and Vacuum Packaging during Storage. Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry, 23(10), 2618.

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Spectral Characteristics of SiRpH4 Compound

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Example 7

The spectral characteristics of compound 3 of the present invention (SiRpH4) were evaluated. The absorption spectrum fluorescence spectrum, and excitation spectrum were measured using a Shimadzu UV-1650PC absorption spectrophotometer and a Hitachi F-4500 fluorometer. The absorption spectra and excitation spectra are shown in FIGS. 4a and 4b.

FIGS. 4a and 4b represent the absorption and excitation spectra of SiRpH4 in 100 mM sodium phosphate buffer (containing 1% DMSO) of different pH. FIG. 4c shows a plot relative to pH of the fluorescence intensity ratio (ratio) when the 700 nm fluorescence intensity when excited at 580 nm was divided by the fluorescence intensity when excited at 663 nm.

SiRpH4 presented the same optical characteristics as SiRpH3, but the pKa of the ratio value change shifted to the basic side in comparison to SiRpH3 due to the ortho position sulfone group.

US10815379B2. pH sensitive fluorescent probe (2020-10-27). The University of Tokyo [JP]. Inventors: Kenjiro Hanaoka [JP], Yu Kagami [JP], Tetsuo Nagano [JP], Yasuteru Urano [JP].

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Fluorescence Spectroscopy of HSA-Ligand Interactions

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Spectra were collected at 25 °C, employing an F-4500 fluorometer (Hitachi, Tokyo, Japan) and a V730 UV-Vis photometer (Jasco, Tokyo, Japan). The effects of mycotoxins and palmitic acid (final concentrations: 0.0, 0.5, 1.0, 2.0, 3.0, 5.0, and 10.0 μM) on the emission spectrum of HSA (2 μM) were tested in phosphate-buffered saline (PBS, pH 7.4), where changes in the emission signals of the protein were evaluated at 340 nm. Based on the UV-Vis spectra, inner-filter effects of ligand molecules were corrected [52 ,53 (link)].

Csenki Z., Bartók T., Bock I., Horváth L., Lemli B., Zsidó B.Z., Angeli C., Hetényi C., Szabó I., Urbányi B., Kovács M, & Poór M. (2023). Interaction of Fumonisin B1, N-Palmitoyl-Fumonisin B1, 5-O-Palmitoyl-Fumonisin B1, and Fumonisin B4 Mycotoxins with Human Serum Albumin and Their Toxic Impacts on Zebrafish Embryos. Biomolecules, 13(5), 755.

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Amyloid Fibril Detection by ThT Assay

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The ThT assay was conducted essentially as described previously [25 (link)]. Ten μl of sample was added to 190 μl of ThT dissolved in 10 mM phosphate buffer, pH 7.4, and then the mixture was vortexed briefly. ThT fluorescence was determined three times at intervals of 10 s using an Hitachi F-4500 fluorometer. Excitation and emission wavelengths were 450 and 482 nm, respectively. Sample fluorescence was determined by averaging the three readings and subtracting the fluorescence of a ThT blank.

Ho L., Ono K., Tsuji M., Mazzola P., Singh R, & Pasinetti G.M. (2017). Protective Roles of Intestinal Microbiota derived Short Chain Fatty Acids in Alzheimer’s Disease-type Beta-Amyloid Neuropathological Mechanisms. Expert review of neurotherapeutics, 18(1), 83-90.

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