An X-4 digital melting-point device was used to determine the melting point, which was not corrected. Using a quartz cuvette with a 10 mm path length, UV-visible spectra were captured by a Shimadzu UV-vis 1800 spectrophotometer. A Hitachi spectrophotometer (RF-6000) was used to capture the fluorescence spectra. 1H NMR and 13C NMR spectra of the ligand were obtained with a Bruker Ultra Shield 400 MHz spectrometer, and the chemical shifts are given in ppm in relation to TMS. With a waters mass spectrometer, ESI-mass spectra were captured using a mixed solvent of HPLC methanol and triple-distilled water. All of the chemicals and metal salts were bought from Merck, and sodium was used as the counter ion for anions and nitrate for metals. In triple-distilled water, solutions of the receptor L (1 × 10−5 M) and metal salts (1 × 10−4 M) were made.
Rf 6000
Manufactured by Hitachi
Sourced in Japan
The RF-6000 is a versatile laboratory equipment designed for radio frequency (RF) analysis and measurement. It serves as a tool for researchers and engineers to characterize and evaluate RF signals and components. The core function of the RF-6000 is to provide accurate and reliable RF data, enabling users to better understand the behavior and performance of their RF systems.
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Lab products found in correlation
4 protocols using rf 6000
1
Spectroscopic Characterization of Ligand Receptor
2
Fluorescence Spectroscopy of Protein Solutions
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The 5 % (w/v) YPs suspensions, including the sonicated samples were diluted to 0.2 % (w/v) with 10 mmol/L phosphate buffer (pH 7.0). Using a fluorescence spectrophotometer (RF-6000, Hitachi Ltd, Tokyo, Japan), the fluorescence emission spectra ranging from 200 to 450 nm were measured while keeping the excitation wavelength fixed at 280 nm. The width of both the excitation slit and the emission slit was set to 5 nm.
3
Fluorescence Spectral Analysis of Complexes
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The fluorescence spectra of the complexes were analyzed by fluorescence spectrophotometer RF-6000 (Hitachi, Japan). The excitation wavelength, emission wavelength and excitation slit were set to 280 nm, 320–460 nm and 5 nm, respectively, and the scanning speed was 2000 nm/min.
4
Measuring Surface Hydrophobicity Using ANS Fluorescence
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The ANS (1-anilino-8-naphthalenesulfonate) fluorescence probe was utilized to measure the surface hydrophobicity, following the approach outlined by Chen, Chen, Ren, and Zhao [41] (link) with minor adjustments. The YPs suspensions were diluted to achieve various concentration (0.25 %, 0. 5 %, 0.75 %, 1 %and 1.25 % w/v) with 10 mM phosphate buffer at pH 7. Next, 20 μL solution of ANS with a concentration of 8 mM was prepared in the identical buffer and subsequently was introduced into the YPs suspensions, with a volume of 4 ml. The mixture was then thoroughly combined. The blends were stored in darkness for a duration of 15 min at ambient temperature. The extrinsic fluorescence intensity was measured using a fluorescence spectrophotometer (RF-6000, Hitachi Ltd, Tokyo, Japan) with an excitation wavelength of 390 nm and the emission spectrum was collected at 470 nm. The H0 was determined by the slope of the regression curve between fluorescence intensity and protein concentration.
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