The largest database of trusted experimental protocols

9 protocols using amx 500 nmr spectrometer

1

Characterization and DFO Release from P(MMD-co-LA) Fiber

Check if the same lab product or an alternative is used in the 5 most similar protocols
AMX-500 NMR spectrometer (Bruker, Germany) was used to detect the DMSO solution's 1H NMR spectrum of P(MMD-co-LA). Evaluated the surface morphology of fiber films by scanning electron microscope (SEM, JSM-IT200, JEOL, Japan), and used ImageJ software (v1.8.0, NIH, USA) to determine the fiber diameter. The mechanical properties of the fiber films were tested by an electronic universal material testing machine (Instron 5967, Instron Corporation, USA). Three sets of parallel samples were set for each characterization.
Prepared DFO solutions of various mass concentrations (1.0, 2.0, 4.0, 8.2, 16.5, 31.6,60.4, 121.7, 250.1, 500.0 ​μg/mL) and chelated them with excess FeCl3 in a volume ratio of 9:1 respectively. Absorbance at 485 ​nm, measured by a microplate reader, drew the standard curve of DFO. Soak 100 ​mg of P(MMD-co-LA)/DFO membrane in 10 ​mL of PBS solution and place it in a shaker at 37 ​°C. Take out 0.9 ​mL of release medium at specific time points (1 ​h, 2 ​h, 4 ​h, 8 ​h, 16 ​h, 24 ​h, 36 ​h, 48 ​h, 60 ​h, 72 ​h, 7th day, 14th day, 21st day, and 28th day) and respectively add them to 0.1 ​mL FeCl3 solution. After mixing well, measure the absorbance at 485 ​nm with a microplate reader to determine the release rate of DFO. Utilized equal volume of PBS to maintain system balance.
+ Open protocol
+ Expand
2

Comprehensive Characterization of Novel Compounds

Check if the same lab product or an alternative is used in the 5 most similar protocols
1H and 13C NMR spectra for compounds were obtained in DMSO-d6, using a Bruker AMX-500 NMR spectrometer. Transmission electron microscopy (TEM) images were obtained on a HITACHI H-7000 FA transmission electron microscope. High-resolution mass spectrometry (HR MS–ESI) spectra were recorded on a Bruker micro TOF-Q instrument. The magnetic properties were measured at 300 K with a vibrating sample magnetometer (SQUID-VSM, Quantum Design, American). In vitro fluorescence images of cells were recorded on a confocal laser scanning microscope (CLSM, Nikon, Japan). The surface areas were measured by an ASAP-2020 physisorption apparatus (Micromeritics, American). The UV–Vis absorption spectra were determined by an Evolution 220 spectrophotometer (Thermofisher Scientific). The size distributions and zeta potentials were measured by a Malvern Zetasizer 90. The metal contents in cells and tissues were tested by ICP-MS (FLEXAR NEXLON300X).
+ Open protocol
+ Expand
3

NMR Analysis of ASPA80-1 Compound

Check if the same lab product or an alternative is used in the 5 most similar protocols
ASPA80-1 (40 mg) was dissolved in 0.5 mL of D2O. After that, NMR (1H NMR and 13C NMR) were recorded by Bruker AMX-500 NMR spectrometer. The parameters of 1H NMR experiment are presented as follows: pulse program zg30, a spectral width of 8.22 kHz, an acquisition time of 4 s, a relaxation delay of 1 s, for 64 scans. For 100 MHz proton decoupled 13C NMR experiment, the parameters are presented as follows: pulse program zgpg30, a spectral width of 24.0 kHz, an acquisition time of 1.36 s, a relaxation delay of 1 s, for 73,728 scans.
+ Open protocol
+ Expand
4

NMR and Mass Spectrometry Analysis Protocol

Check if the same lab product or an alternative is used in the 5 most similar protocols
Solvents used were of analytical or HPLC grade and were purchased from Merck (Darmstadt, Germany). The 1H and 13C NMR analyses were run on a Bruker AMX-500 NMR spectrometer (Karlsruh, Germany), operating at 400 MHz for 1H and 125 MHz for 13C NMR, respectively. DMSO-d6 as solvent and tetramethyl silane (TMS) as internal standard were used. HR-ESIMS analysis was carried out with an LCT Premier XE Micromass Waters spectrometer in the positive and negative ionization modes (Waters Corporation). Detection of compounds was carried out on precoated silica gel 60 F254 plates (0.25 mm layer, E. Merck, Darmstadt, Germany), using chloroform–methanol–water (8:2:0.2) as a mobile phase, and visualized with 5% H2SO4 spray reagent after heating at 110 °C.
+ Open protocol
+ Expand
5

NMR Characterization of Polysaccharides

Check if the same lab product or an alternative is used in the 5 most similar protocols
The 1H and 13C nuclear magnetic resonance (NMR) spectra of the CMC, SCMC, κ-carrageenan, and CM-κ-Car samples were recorded on a Bruker AMX-500 NMR spectrometer at ambient temperature. The samples were dissolved in D2O (35 mg/ml). Chemical shifts (in ppm) were expressed relative to the resonance. MestreNova software (Version 9.0, Mestrelab Research S.L., Santiago de Compostela, Spain) was used to process the data, which included a 90° shifted square sine-bell apodization window. Baseline and phase correction were conducted in both directions.
+ Open protocol
+ Expand
6

Comprehensive Spectroscopic Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
Ultraviolet spectra were recorded on a Hitachi UV 3200 spectrophotometer in MeOH. Infrared spectra were recorded on a JASCO 302-A spectrophotometer. EI-MS, were recorded on a Finnigan MAT 95 spectrometer (70 eV) with perfluorokerosene as reference substance for EI-HR-MS. The 1 H and 13 C NMR spectra were recorded on Bruker AMX 500 NMR spectrometer.
Chemical shifts are reported in δ (ppm) using TMS as internal standard and coupling constants (J) were measured in Hz. Column chromatography was carried out on silica gel (70-230 mesh, Merck). Thin layer chromatography (TLC) was performed on Merck precoated silica gel 60 F 254 aluminium foil, and spots were detected using ceric sulphate spray reagent.
+ Open protocol
+ Expand
7

Spectroscopic Analysis of Compounds 1-3

Check if the same lab product or an alternative is used in the 5 most similar protocols
The 1 H NMR and 13 C NMR spectra were recorded on a Bruker AMX-500 NMR spectrometer (Bruker, Karlsruhe, Germany). 1 H NMR chemical shifts were referenced to the residual CDCl 3 solvent peak at δ7.24 ppm, and 13 C NMR chemical shifts were referenced to the CDCl 3 solvent peak at δ77.0 ppm. HR-FDMS results were recorded on a JEOL JMS T100GCV mass spectrometer (Jeol, Tokyo, Japan). The NMR spectroscopic data of compounds 1-3 are shown in the Supplemental data.
+ Open protocol
+ Expand
8

NMR Spectroscopy of Compound Characterization

Check if the same lab product or an alternative is used in the 5 most similar protocols
The 1 H, 13 C, and 29 Si NMR spectra were recorded in CDCl 3 /CD 2 Cl 2 or CDCl 3 /[D 6 ]acetone solutions using a Bruker AMX 500 spectrometer at 500, 126, and 99 MHz, respectively, unless otherwise stated. The 29 Si{ 1 H} NMR INEPT spectra were recorded using a Bruker AMX 500 NMR spectrometer at 99 MHz, while 29 Si{ 1 H} inverse-gated NMR spectra were recorded on a Bruker Avance 600 spectrometer at 119.23 MHz. Chemical shifts for all NMR spectra are reported in ppm relative to TMS.
+ Open protocol
+ Expand
9

Copper(II) Complexes: Characterization and Bioactivity

Check if the same lab product or an alternative is used in the 5 most similar protocols
All the chemicals used in the study were purchased from sigma Aldrich and used without further purification after having been dried according to the standard procedures [30] . The ligands and [CuCl2(PPh3)2] were prepared according to the literature methods [31, 32] . Infrared spectra of the ligand and the metal complexes were recorded as KBr discs over the range of 4000-400 cm -1 using a Jasco FT-IR 4100 FT-IR spectrophotometer. The melting points were recorded with a Lab India Melting point apparatus and elemental analyses (CHNS) were performed on a Vario EL III Elementar analyser instrument. The electronic spectra of the complexes were recorded with a Jasco V-630 spectrophotometer and emission spectra were measured using a Jasco FP 6600 spectrofluorometer. 1 H NMR spectra were recorded on a Bruker AMX 500 NMR spectrometer at 500 MHz. DNA binding, viscometry, Ethidium bromide replacement, Protein binding and cytotoxicity experiments were carried out by strictly following the procedures reported in the literature [33] [34] [35] [36] [37] .
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!