The largest database of trusted experimental protocols

66 protocols using uv visible spectrophotometer

1

Characterization of Synthetic Compounds

Check if the same lab product or an alternative is used in the 5 most similar protocols
NMR spectra were recorded in a Bruker AV400 (1H-NMR at 400 MHz, 13C{1H} NMR at 100.6 MHz and 31P{1H} NMR at 161.9 MHz. Chemical shifts (δ) are given in ppm using CDCl3 as the solvent, unless otherwise stated. 1H and 13C NMR resonances were measured relative to solvent peaks considering tetramethylsilane = 0 ppm, and 31P{1H} NMR was externally referenced to H3PO4 (85%). Coupling constants J are given in hertz. IR spectra (4000250 cm−1) were recorded on a Nicolet 6700 Fourier transform infrared spectrophotometer on solid state (ATR accessory). Elemental analyses were performed on a Perkin-Elmer 2400 CHNS/O series II analyzer. Mass (MS) spectra (electrospray ionization, ESI) were performed on a Waters Q-Tof Ultima. Stability studies were performed in a Cary 100 Bio UV-visible spectrophotometer. The pH was measured in an OAKTON pH conductivity meter in 1:99 DMSO/H2O solutions.
+ Open protocol
+ Expand
2

Spectrophotometric Assay for HOCl Detection

Check if the same lab product or an alternative is used in the 5 most similar protocols
A Cary 100 Bio UV–visible spectrophotometer was used to record the absorbance spectra, at 25°C, pH 7.0. Experiments were performed in a 1-ml phosphate buffer solution (200 mM, pH 7.4), and then supplemented with fixed amount of (CN)2-Cbi (10 µM) followed by increasing concentrations of HOCl. Reaction completion was assured after 2 hours of incubation, and methionine (5-fold of the final HOCl concentration) was added to eliminate excess HOCl, and absorbance changes were recorded from 300 to 700 nm.
+ Open protocol
+ Expand
3

Spectroscopic Characterization of Organic Compounds

Check if the same lab product or an alternative is used in the 5 most similar protocols
NMR spectra were recorded in a Bruker AV400 (1H-NMR at 400 MHz, 13C{1H} NMR at 100.6 MHz and 31P{1H} NMR at 161.9 MHz. Chemical shifts (δ) are given in ppm using CDCl3 as the solvent, unless otherwise stated. 1H and 13C NMR resonances were measured relative to solvent peaks considering tetramethylsilane = 0 ppm, and 31P{1H} NMR was externally referenced to H3PO4 (85%). Coupling constants J are given in hertz. IR spectra (4000 to 250 cm−1) were recorded on a Nicolet 6700 Fourier transform infrared spectrophotometer on solid state (ATR accessory). Elemental analyses were performed on a Perkin-Elmer 2400 CHNS/O series II analyzer. Mass (MS) spectra (electrospray ionization, ESI) were performed on a Waters Q-Tof Ultima. Stability studies were performed in a Cary 100 Bio UV-visible spectrophotometer. The pH was measured in an OAKTON pH conductivity meter in 1:99 DMSO/H2O solutions.
+ Open protocol
+ Expand
4

Mucin Adsorption on Coated C-PLGA NPs

Check if the same lab product or an alternative is used in the 5 most similar protocols
Adsorption of pig mucin (PM) on the surface
of noncoated and chitosan, WGA-, and GE11-coated C-PLGA NPs was determined
by slightly modifying the method reported by Yin et al.43 (link) Briefly, 1 mL of mucin suspension (1 mg/mL)
in PBS with pH 7.4 was stirred with 1 mL of each C-PLGA NP formulation
for 2 h at 37 °C. Then, the suspensions were centrifuged at 25 000g for 1 h. The amount of free PM in the supernatant was
determined by measuring the absorbance value at 260 nm by using a
UV spectrophotometer (UV Visible Spectrophotometer, Cary 100 Conc,
Australia). The amount of adsorbed PM was calculated by using a standard
curve measured for known amounts of PM in PBS. The calibration curve
for mucin in PBS was determined with a series of mucin standard solutions
with concentrations of 30, 60, 125, 250, 500, 750, and 850 μg/mL.
The PM binding efficiency of the different C-PLGA NPs was calculated
from the following equation where C0 is the
initial concentration of PM used for incubation and Cs is the concentration of free PM determined in the supernatant.
+ Open protocol
+ Expand
5

Spectrophotometric Protein Quantification

Check if the same lab product or an alternative is used in the 5 most similar protocols
UV-visible absorbance spectra were recorded using a Cary UV-visible
spectrophotometer. Protein concentrations were estimated from A280using their respective absorbance coefficients, which were calculated from their
primary amino acid sequence using the ProtParam program on the ExPASy proteomics
server. Wild type and E49Q P. aeruginosa UbiX
ε280 = 16960M-1 cm-1, Y169F
ε280 =15470 M-1 cm-1 and W200F
ε280 = 11460M-1 cm-1. The
concentration of A.niger Fdc1 and FMN were estimated using
ε280 = 68870M-1 cm-1 and
ε450 = 12500M-1 cm-1respectively.
+ Open protocol
+ Expand
6

Quantifying Erv1 FAD Reduction Dynamics

Check if the same lab product or an alternative is used in the 5 most similar protocols
Electron titrations of the FAD cofactor in Erv1 were conducted in BAE using protein concentrations (based on bound FAD) ranging from 30 to 60 μm. A freshly made sodium dithionite solution was titrated using an anaerobic FAD solution of known concentration (ε450 = 11.3 mm−1·cm−1). This titration was done before and after the Erv1 assays to obtain an average normality. Small known volumes (0.5–2 μL) of dithionite solution were then used to reduce the protein. The UV‐visible spectrum was recorded from 250 to 700 nm after each addition (equilibration time of 10–15 min) using a Cary 50 Bio UV‐visible spectrophotometer. The point at which the reduction of FAD was completes (no further decrease in absorbance at either 460 marked the number of electrons required for complete FAD reduction. The relative absorbance change at 460 was normalised with the value of the fully oxidised FAD set as 1 and the value of the fully reduced FAD as 0. The results are the average of two independent experiments.
+ Open protocol
+ Expand
7

Isolation and Characterization of Rat Hepatocyte DNA

Check if the same lab product or an alternative is used in the 5 most similar protocols
Rat hepatocyte double stranded DNA (dsDNA) was isolated by standard phenol-chloroform method. DNA stock solution was prepared in Na2HPO4-NaH2PO4 (0.1 M) buffer and stored at 20 °C. DNA concentration and quality was evaluated by NanoDrop (thermoscientific-USA) and UV-Visible spectrophotometer (Cary 100 Bio-model, Australia). UV-Visible spectra of ZEO were recorded using spectrophotometer in phosphate buffer (0.1 M with pH = 7.4) at room temperature over a wavelength range 190–600 nm. Initially the absorbance of ZEO concentrations ranging from 0 to 32 μg/ml in phosphate buffer at 298 K was measured, the solvent was taken as reference, and then similar procedure was carried out after addition of constant DNA concentration (50 μg/ml).
+ Open protocol
+ Expand
8

Characterization of Mesoporous Bioactive Glass

Check if the same lab product or an alternative is used in the 5 most similar protocols
Elemental analysis data were collected by a PerkinElmer 2400 CHNS analyzer, the results are expressed as % (w/w) of the drug with respect to the bioactive glass.
Specific surface area (SSA) and porosity were evaluated for MBG glass before and after soaking in ethanol solution and evaporation under vacuum. Measurements were performed by N2 adsorption at −196 °C using a Micromeritics ASAP 2020 porosimeter. For SSA determination, data were processed by employing the BET model. The BJH model was used to analyze mesopores size distribution, and the “t-plot” (statistical thickness method) was adopted to evaluate the presence of micropores [42 (link),43 (link)]. For a review of the applied methods, see Gregg and Sing [44 ]. Before N2 adsorption measurements, all samples were outgassed at rt for 24 h (residual pressure: ~10−3 Torr).
The UV-Vis spectra of the solutions were collected using a Cary 100 UV-visible spectrophotometer in the 200–600 nm range.
+ Open protocol
+ Expand
9

Spectrophotometric Protein Quantification

Check if the same lab product or an alternative is used in the 5 most similar protocols
UV-visible absorbance spectra were recorded using a Cary UV-visible
spectrophotometer. Protein concentrations were estimated from A280using their respective absorbance coefficients, which were calculated from their
primary amino acid sequence using the ProtParam program on the ExPASy proteomics
server. Wild type and E49Q P. aeruginosa UbiX
ε280 = 16960M-1 cm-1, Y169F
ε280 =15470 M-1 cm-1 and W200F
ε280 = 11460M-1 cm-1. The
concentration of A.niger Fdc1 and FMN were estimated using
ε280 = 68870M-1 cm-1 and
ε450 = 12500M-1 cm-1respectively.
+ Open protocol
+ Expand
10

Excited State Recovery Kinetics

Check if the same lab product or an alternative is used in the 5 most similar protocols
Excited state recovery times were measured using a Cary 50 UV-Visible Spectrophotometer. Samples were irradiated with blue light (6.0 mW cm−2 blue light, collimated blue led array) and absorbance at 450 nm was recorded until recovery.
+ 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!