F 4500 fluorimeter

Manufactured by Hitachi

Sourced in Japan

The F-4500 fluorimeter is a laboratory instrument designed to measure the fluorescence intensity of samples. It is capable of exciting samples at a selected wavelength and detecting the resulting fluorescent emission. The F-4500 provides accurate and reliable measurements of fluorescence properties, making it a valuable tool for various scientific applications.

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Lab products found in correlation

8453 spectrometer, by Agilent Technologies (1 mentions) Fls980, by Edinburgh Instruments (1 mentions) Cs from porcine heart, by Merck Group (1 mentions) Ethanol, by Reanal (1 mentions) Sbfi am, by Thermo Fisher Scientific (1 mentions)

19 protocols using f 4500 fluorimeter

Fluorescent Colorimetric Dish Analysis

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To a disposable fluorescent colorimetric dish, the aqueous solution of PT-OH-PPR (30 μM, 1 mL) was added. To another disposable fluorescent colorimetric dish, an aqueous solution of Lysotracker Red DND-99 (10 μM, 1 mL) was added. The above samples were irradiated under white light (6 mW cm⁻², 12 min), meanwhile, their fluorescence intensity was recorded every two minutes using a Hitachi F-4500 fluorimeter.

Wang F., Xia H., Pu S., Yan N., Song J., Tian Y., Wei J, & Yan L. (2019). Novel polythiophene derivative for dual-channel cell imaging. RSC Advances, 9(30), 17335-17340.

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Fluorescence Spectroscopy of Z14G-CD Complexes

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Steady-state fluorescence spectroscopic measurements were carried out at +25 °C, in the presence of air, using a Hitachi F-4500 fluorimeter (Hitachi, Tokyo, Japan). Fluorescence emission spectra of Z14G (1 µM) was recorded in the absence and presence of increasing concentrations of CDs (0.0, 0.2, 0.3, 0.5, 0.7, 1.0, 1.5, and 2.0 mM) in different buffers (pH 3.0–10.0; see 2.1), applying 315 nm excitation wavelength. Binding constants of Z14G-CD complexes were determined employing the graphical application of the Benesi-Hildebrand equation [26 (link)]:

\frac{I_{0}}{(I - I_{0})} = \frac{1}{A} + \frac{1}{A \times K \times {[H]}^{n}}

where I₀ and I denote the fluorescence emission intensities of Z14G in the absence and presence of CDs, respectively; A is a constant, K is the binding constant (unit: L/mol), [H] is the concentration of the host molecule, and n is the number of binding sites.

Faisal Z., Fliszár-Nyúl E., Dellafiora L., Galaverna G., Dall’Asta C., Lemli B., Kunsági-Máté S., Szente L, & Poór M. (2019). Cyclodextrins Can Entrap Zearalenone-14-Glucoside: Interaction of the Masked Mycotoxin with Cyclodextrins and Cyclodextrin Bead Polymer. Biomolecules, 9(8), 354.

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Spectroscopic Characterization of Organometallic Complexes

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IR spectra were recorded on a Mattson RS FTIR instrument, averaging 64 scans at resolution 2 cm^–1. ATR-IR spectra were an average of 32 scans. UV/visible absorption spectra were measured using an Agilent 8453 spectrometer. Steady state emission spectra were measured using a Hitachi F-4500 fluorimeter. The fluorescence was taken against a ZnTPP reference for the bromide complexes and against the individual dyad ligand ZnTPP-link-Bpy for the picoline complexes. Time-resolved emission was measured with an Edinburgh Instruments FLS980 equipped with a 560 nm pulsed LED (EPLED 560, pulsewidth 1.5 ns) and a red PMT detector. All samples were either degassed by three freeze–pump–thaw cycles or de-aerated by purging the sample with Ar. Correction was applied for instrument response. All absorption and emission measurements were made in 10 × 10 mm quartz cuvettes.

Windle C.D., George M.W., Perutz R.N., Summers P.A., Sun X.Z, & Whitwood A.C. (2015). Comparison of rhenium–porphyrin dyads for CO2 photoreduction: photocatalytic studies and charge separation dynamics studied by time-resolved IR spectroscopy †Electronic supplementary information (ESI) available: NMR spectra, cyclic voltammograms, crystallographic data, fluorescence data, spectra from photoreactions and photocatalytic data. CCDC 1406000 and 1406001. For ESI and crystallographic data in CIF or other electronic format see DOI: 10.1039/c5sc02099a. Chemical Science, 6(12), 6847-6864.

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Chaperone Activity of Hsp33 on Denatured Citrate Synthase

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Preparation of reduced, inactive Hsp33 (Hsp33_red) or HOCl-oxidized active Hsp33 (Hsp33_ox), and chaperone-activity measurements using either chemically or thermally denatured citrate synthase (CS) as client protein16 (link). To test the effects of Hsp33 on chemically denatured clients, CS from porcine heart (Sigma-Aldrich) was denatured to a final concentration of 12 μM in 6.0 M guanidinium-hydrochloride (GdmCl), 40 mM HEPES (pH 7.5) overnight at room temperature. To initiate aggregation of CS, the unfolded enzyme was diluted 1:160 into 1,600 μl 40 mM HEPES (pH 7.5) at either 20 or 30 °C in the absence or presence of Hsp33. To analyse Hsp33's effects on thermally unfolding CS, 0.15 μM CS were incubated in 1,600 μl 40 mM HEPES (pH 7.5) at the indicated temperatures in the absence or presence of Hsp33. For both assays, light scattering was monitored using a Hitachi F4500 fluorimeter equipped with a thermostated cell holder and stirrer. Excitation and emission wavelengths were set to 360 nm, and the excitation and emission slit widths were set to 2.5 nm. For competition studies between CS and NPY/NPY D4C IAM-TEMPO, a 10-fold molar excess of peptide to CS was used and the assay performed as described.

Groitl B., Horowitz S., Makepeace K.A., Petrotchenko E.V., Borchers C.H., Reichmann D., Bardwell J.C, & Jakob U. (2016). Protein unfolding as a switch from self-recognition to high-affinity client binding. Nature Communications, 7, 10357.

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Chaperone Activity of Hsp33 on Denatured Citrate Synthase

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Chaperone activity measurements with chemically denatured citrate synthase from porcine heart (CS, Sigma-Aldrich) were conducted as previously described (Ilbert et al., 2007 (link)). In short, CS was denatured to a final concentration of 12 μM in 6.0 M Gdn*HCl, 40 mM HEPES, pH 7.5 overnight at room temperature. To initiate aggregation of CS, the unfolded enzyme was diluted 1:160 into 40 mM HEPES, pH 7.5 at 30°C in the absence or presence of various concentrations of reduced or oxidized Hsp33. Light scattering was monitored using a Hitachi F4500 fluorimeter equipped with a thermostated cell holder and stirrer. Excitation and emission wavelengths were set to 360 nm, and the excitation and emission slit widths were set to 2.5 nm.

Groitl B., Dahl J.U., Schroeder J.W, & Jakob U. (2017). Pseudomonas aeruginosa defense systems against microbicidal oxidants. Molecular microbiology, 106(3), 335-350.

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Steady-State Emission Spectrum of MG

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Steady-state emission spectrum and phosphorescence lifetime were obtained at 77 K in a Hitachi-F4500 fluorimeter equipped with a Quartz Dewar for liquid nitrogen. The MG stock solution (12.9 mM) in ethanol was placed in a capped 5 mm diameter NMR tube and rapidly cooled in liquid nitrogen.

Yamagata K., Kato J.I., Shimamoto A., Goto M., Furuichi Y, & Ikeda H. (1998). Bloom’s and Werner’s syndrome genes suppress hyperrecombination in yeast sgs1 mutant: Implication for genomic instability in human diseases. Proceedings of the National Academy of Sciences of the United States of America, 95(15), 8733-8738.

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Nile Red Fluorescence Assay for C7E2 and C7K3

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Solutions of C₇E₂ and C₇K₃ were prepared as specified in the General Conditions section and adjusted to pH 7.5 using 0.1 M NaOH and HCl solutions. On the day of measurement, these solutions were serial diluted to triplicate sets of 1 mM, 0.5 mM, 0.25 mM, 0.1 mM, 0.04 mM, and 0.008 mM concentrations using a preadjusted 150 mM NaCl solution with a total volume of 1 mL. A solution of Nile red was prepared at 150 μM in ethanol. A micropipette calibrated to the density of ethanol was used to dispense 1 μL of Nile red solution in each sample. These samples were then agitated briefly and allowed to incubate at room temperature for 2 h. The solutions were then analyzed using a Hitachi F-4500 fluorimeter operating at a 550 nm excitation wavelength. Each acquisition was the average of three scans in a 5 × 5 mm quartz cuvette.

Preslar A.T., Tantakitti F., Park K., Zhang S., Stupp S.I, & Meade T.J. (2016). 19F Magnetic Resonance Imaging Signals from Peptide Amphiphile Nanostructures Are Strongly Affected by Their Shape. ACS nano, 10(8), 7376-7384.

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Fluorescence-based Determination of Binding Constants

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Steady-state fluorescence measurements were carried out using a Hitachi F-4500 fluorimeter. The experiments were performed in a wide pH range (1.0–10.0; see details in 3.1). All analyses were carried out in the presence of air at +25 °C. Fluorescence spectra were recorded in the presence of DHC (2 μM) and increasing concentrations of CDs (0.0, 0.2, 0.5, 1.0, 1.5, and 2.0 mM), employing 325 and 410 nm as excitation and emission wavelengths, respectively.
Binding constants (K) of DHC-CD complexes were determined by the graphical application of the Benesi-Hildebrand equation, assuming 1:1 stoichiometry [19 (link)]:

\frac{I_{0}}{(I - I_{0})} = \frac{1}{A} + \frac{1}{A \times K \times {[H]}^{n}}

where I is the fluorescence intensity of DHC in the presence of CD, I₀ is the fluorescence intensity of DHC in the absence of CD, [H] stands for the concentration of CDs, A is a constant, n is the number of binding sites, and K (unit: L/mol) denotes the binding constant.

Faisal Z., Kunsági-Máté S., Lemli B., Szente L., Bergmann D., Humpf H.U, & Poór M. (2019). Interaction of Dihydrocitrinone with Native and Chemically Modified Cyclodextrins. Molecules, 24(7), 1328.

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Zinquin Acid Fluorescence Measurement

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Fluorescence measurements were carried out on a Hitachi F-4500 fluorimeter. The excitation wavelength for Zinquin acid (ZQ) was 370 nm and emission spectra were obtained over the spectral range of 400 to 600 nm. All fluorescence spectra were recorded in arbitrary units at room temperature and corrected for the background fluorescence

Namdarghanbari M.A., Bertling J., Krezoski S, & Petering D.H. (2014). Toxic Metal Proteomics: Reaction of the Mammalian Zinc Proteome with Cd2+. Journal of inorganic biochemistry, 136, 115-121.

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Fluorescence Quenching Analysis of HSA

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Fluorescence spectra were recorded on a Hitachi-F4500 fluorimeter in 1 cm quartz cell at 25.0 ± 0.1 °C. All solutions were prepared in PBS' (pH 7.40) and were incubated for 15 min or 24 h. Samples contained 1 M HSA and various HSA-to-ligand or metal ion or metal complex ratios (from 1:0 to 1:10) were used. The excitation wavelength was 295 nm and the emission was read in the range of 305-450 nm. The quenching constant (log K'Q) was calculated with the computer program PSEQUAD [63] using the same approach applied in our previous works [28, 29] (link).
Samples were separated by ultrafiltration through 10 kDa membrane filters (Microcon YM-10 centrifugal filter unit, Millipore) in low (LMM) and high molecular mass (HMM) fractions with the help of a temperature controlled centrifuge (Sanyo, 10000/s, 10 min).
Samples (0.50 mL) contained 50 M HSA and Rh( 5 -C5Me5) or its acac complex (150 M) in PBS' buffer (pH 7.30) at 25.0 ± 0.1 °C and were incubated for 24 h. The LMM fraction

Mészáros J.P., Poljarevic J.M., Gál G.T., May N.V., Spengler G, & Enyedy É.A. (2019). Comparative solution and structural studies of half-sandwich rhodium and ruthenium complexes bearing curcumin and acetylacetone. Journal of inorganic biochemistry, 195.

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