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J 810 spectrometer

Manufactured by Jasco
Sourced in Japan, United States, Germany

The J-810 spectrometer is a versatile instrument designed for spectroscopic analysis. It is capable of performing precise measurements of the interaction between light and matter, allowing for the characterization of a wide range of samples. The core function of the J-810 is to accurately detect and measure the absorption, emission, or reflectance properties of materials across a specific range of the electromagnetic spectrum.

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87 protocols using j 810 spectrometer

1

Spectroscopic Analysis of Organic Compounds

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The UV spectra, optical rotations, and IR spectra were determined on a JASCO V-550 UV/VIS spectrophotometer in MeOH solutions, an Autopol JASCO P-1020 polarimeter with concentrations unit reported in g/100 ml, a JASCO FT/IR-480 plus FT-IR spectrometer with KBr disks and peaks reported in cm−1 (JASCO corporation, Tokyo, Japan), respectively. ECD spectrum were carried out on a JASCO J-810 spectrometer. NMR experiments including 1D and 2D spectra were run on a Bruker Avance 600 NMR (600 MHz for 1H/150 MHz for 13C) spectrometer using standard Bruker pulse sequences (Bruker-Biospin, United States). HRESIMS data were measured from an Agilent 6210 LC/MSD Q-TOF mass instrument (Agilent Technologies, CA, United States). Analysis and preparation of crude samples were performed on HPLC using Shimadzu 6AD series with a PDA detector (Shimadzu corporation, Tokyo, Janpan). Al2O3 thin layer chromatography (TLC) analysis was done on aluminium oxide 60 F 254 basic plates (Merck, China). Column chromatography (CC) was undertaken with D-101 macroporous resin (Diaion, Shanghai, China), simon alumina N (size 200–300 mesh, Aldrich, China), Sephadex LH-20 (size 25–100 mm, Fluka, Buchs, Switzerland), CHP20P MCI gel (size 75–150 μm, Sigma-Aldrich company Ltd. China), and ODS silica gel (size 50 mm; YMC, Tokyo, Japan).
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2

Characterization of LLO Secondary Structure

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LLO secondary structures in the presence or absence of atractylodin (4 μg/mL) were characterized using CD spectroscopy. Briefly, CD spectra were acquired by recording spectra at the scanning wavelengths ranging from 190-250 nm at a 0.5 nm interval using a Jasco J-810 spectrometer and analyzed via the BeStSel web server (https://bestsel.elte.hu/index.php).
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3

Circular Dichroism Analysis of Peptide Structures

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Peptide structures in solution were acquired by circular dichroism measurement in water and 30% TFE mix. The spectra were obtained on a JASCO J-810 spectrometer at room temperature. Data was assessed at 190 to 260 nm wavelength using 20 nm/min scan rate and 1 nm band with. The data was collected using Spectra Manager Software and analysed using SELCOM3, CONTILL and CDSSTR database [19] (link).
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4

Circular Dichroism of α-Synuclein with CL

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A Jasco J-810 spectrometer was used for CD measurements. Samples containing 10 µM WT α-Syn alone and in the presence of CL (80 µM and 160 µM) were prepared in a 25 mM phosphate buffer (pH 7.4) and measured immediately after mixing. Experiments were performed at 25 °C using a quartz glass cell with 1-mm path length. The samples were recorded from 190 nm to 260 nm wavelength with a total of three scans for each sample.
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5

Characterization of Purified HFn Proteins

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Purified HFn‐based proteins were buffer exchanged into 20 mM PB, pH 7 and their concentrations were adjusted to 0.2 mg/mL for CD and IF analysis. CD spectroscopy was measured on a J‐810 spectrometer (Jasco, Japan) at 25°C using a 1.0 mm path length quartz cuvette. The wavelength scanning was conducted from 260 to 190 nm at a rate of 500 nm/min with a bandwidth of 1 nm. The average of three scans of each sample was presented. IF spectroscopy was performed on F‐4500 fluorescence spectrophotometer (Hitachi, Japan). The excitation wavelength was 280 nm and the emission was recorded from 300 to 400 nm with a scanning rate of 1200 nm/min. 1.0 cm path length cuvette was used. Each sample was also subjected to scan for three times.
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6

Spectroscopic Characterization of Compounds

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Optical rotations were measured on a JASCO P-200 polarimeter (Tokyo, Japan). The UV spectra were recorded in methanol using a Shimadzu UV-260 spectrophotometer (Kyoto, Japan). The ECD spectra were measured by a JASCO J-810 spectrometer (Tokyo, Japan). The IR measurements were performed on a Perkin-Elmer 683 spectrometer. The NMR experiments were conducted on Bruker Avance III-600 MHz spectrometers in CDCl3 and DMSO-d6. The HR ESIMS data were acquired using a Thermo Fisher Q-Exactive mass spectrometer (Boston, USA). Column chromatography (CC) separations were carried out by using silica gel (300–400 mesh; Qingdao Haiyang Chemical Co., Ltd., Qingdao, China), and ODS RP-C18 (40–63 μm, FuJi, Aichi, Japan). An Agilent 1260 series system (California, USA) with an COSMOSIL 5C18-MS-II (5 μm, 4.6 mm i.d. × 150 mm, Kyoto, Japan) column was used for HPLC analysis. Preparative HPLC was carried out using a Welch Sail 1000 series instrument equipped with a Welch Ultimate XB-C18 column (5 μm, 250 mm × 21.2 mm i.d., China).
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7

Amylin Secondary Structure Characterization

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In conjunction with the ThT assay, changes on the secondary structure of amylin in the presence of the different peptide conjugates were done using CD spectroscopy on a Jasco J-810 spectrometer (Easton, MD). Similar solutions as with the ThT assay in the absence of thioflavin t were prepared with the CD spectra taken every 30 min for 24 h. All CD spectra were subtracted with the CD spectra of a blank containing 40 μM peptide conjugate in 10 mM Tris-HCl buffer (pH 7.5).
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8

Characterizing rhEPO Secondary Structure

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Circular Dichroism Spectroscopy (CD) spectra of rhEPO and AD-rhEPO powder samples were collected at 25°C with a J-810 Spectrometer (Jasco, Japan) at the wavelength range of 190 - 350 nm. Distilled water was used to prepare solutions with a concentration of 0.2 mg/mL. For the measurement in the far-UV area, the path length of the cuvette was 1 mm. After scanning each spectrum three times, the average spectrum was plotted. Far-UV-CD measurements were performed to investigate the effect of the linker (AD) on the secondary structure of rhEPO.
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9

Quantitative Circular Dichroism Spectroscopy

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CD spectra were recorded on a Jasco J-810 spectrometer. CD spectra of aqueous 6-thioguanosine (1 mg ml−1) were recorded in a quartz cell with pathlength 0.2 mm. CD spectra of 1 as a gel (prepared with 10 mg/1.8 ml of 6-thioguanosine) were recorded in a quartz cuvette of pathlength 0.1 mm. In order to facilitate direct, quantitative comparison of the two samples, the ellipticity for the 6-thioguanosine (Supplementary Fig. 4a) has been multiplied by a factor 10/3.6 to account for the difference in concentration and pathlength.
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10

Circular Dichroism Analysis of Exenatide in PLGA Microspheres

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Circular dichroism spectroscopy was conducted on a Jasco J‐810 spectrometer (Jasco, Japan) using a 0.1 cm path cuvette with a scan rate of 50 nm/min at 30°C. For extracting exenatide from solid PLGA microspheres, microspheres equivalent to 10 mg exenatide were dissolved in 3 ml acetonitrile using a vortex mixer; then, 3 ml of acetate buffer solution (pH 4.5, 30 mM) was added and immediately vortexed to precipitate the PLGA polymer. The suspension obtained after acetonitrile removal by rotary evaporation under vacuum was centrifuged (1730 MR, GYROZEN Co. Ltd., Korea) at 12,000 rpm for 5 min to separate the precipitated PLGA polymer. The collected supernatant was used as the sample solution for CD spectroscopy. For comparing secondary structural integrity, raw exenatide solution (10 mg/3 ml) in acetate buffer (pH 4.5, 30 mM) was used as a control. A total of 24 scans were performed, and the averaged spectrum was used for secondary structural analysis.
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