The catalase activity of IgGs was determined out according to Aebi [53 (link)]. The reaction was run by adding 100 μl IgGs (concentration 0.5 mg/ml) to the incubation mixture (50 mM potassium phosphate (pH 7.0), 30 mM H2O2). The catalase activity of IgGs was determined spectrophotometrically from a decrease of absorbance at 240 nm for 5-8 min caused by the splitting of hydrogen peroxide using Lambda 45 spectrophotometer (Perkin Elmer). All measurements were taken within the linear regions of the time courses and linear part of relative activity dependence upon IgG concentration. For the calculation of the activity, the molar extinction coefficient of hydrogen peroxide (ε = 0.081 mM−1/cm−1) was used [53 (link)]. The measured relative activities for IgGs were normalized to standard conditions (mM Н2О2/min/mg IgGs).
Lambda 45 spectrophotometer
Manufactured by PerkinElmer
Sourced in United States
The Lambda 45 spectrophotometer is a high-performance UV-Vis instrument designed for accurate and reliable analysis. It features a double-beam optical system and a wide wavelength range of 190 to 900 nanometers. The instrument is capable of performing a variety of spectroscopic measurements, including absorbance, transmittance, and reflectance.
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Lab products found in correlation
Jobin yvon fluoromax 4 spectrofluorimeter, by Horiba (1 mentions)
Thermogravimetric analyzer, by PerkinElmer (1 mentions)
Prestige 21, by Shimadzu (1 mentions)
Alpha ftir spectrophotometer, by Bruker (1 mentions)
Ls55 spectrofluorimeter, by PerkinElmer (1 mentions)
Zetasizer nano series, by Malvern Panalytical (1 mentions)
Milli q system, by Merck Group (1 mentions)
Purine nucleoside phosphorylase, by Merck Group (1 mentions)
A3782, by Merck Group (1 mentions)
A7085, by Merck Group (1 mentions)
F 7000 spectrofluorometer, by Hitachi (1 mentions)
J 815 spectropolarimeter, by Jasco (1 mentions)
Polyethylene oxide, by Merck Group (1 mentions)
Mcr 302, by Anton Paar (1 mentions)
16 protocols using lambda 45 spectrophotometer
1
Catalase Activity Assay of IgGs
2
Photophysical Characterization of Nanoparticles
3
Leaf Pigment and Nitrogen Analysis
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Immediately after the last leaf had fully expanded, 20 leaves were obtained from each plot. Ten of the collected leaves were extracted using 96% (v/v) ethanol, and their chlorophyll concentrations were determined by measuring absorbance at 649 and 665 nm using a Lambda 45 spectrophotometer (Perkin-Elmer, USA). The remaining leaves were dried at 70°C until a constant weight, and leaf N concentrations were then determined by the Dumas combustion method [20] on a Rapid N Cube nitrogen analyzer (Elementar, Germany). Leaf N and chlorophyll concentrations were measured four times at 10-d intervals.
4
Characterization of Coated Fe3O4 Nanoparticles
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FT-IR spectra (Shimadzu prestige-21) were used to determine the identity of the as prepared nanoparticles and to characterize the coated Fe3O4 nanoparticles. X-ray powder diffraction measurements were performed using an X-ray diffractometer (XRD) (Perkin Elmer) at ambient temperature. The surface morphology of the silica-supported ligands was identified with a scanning electron microscope (LECO SEM, Michigan, USA). Magnetic measurements were performed by means of the vibrating sample magnetometery method, using a VSM 7407 magnetometer, at room temperature. Thermogravimetric analysis (TGA) was performed using a Perkin Elmer thermogravimetric analyzer. UV–Visible spectra in the 200–1000 nm range were obtained in DMF solvent on a Perkin Elmer Lambda 45 spectrophotometer. A Jenway model 4510 pH-meter was used for pH measurements by use of a combined electrode. An ultrasonication probe (Karl Deutsch, Germany) was used to disperse the nanoparticles in the solution.
5
Characterization of Complexes by Analytical Techniques
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Carlo Erba model 1106 elemental analyzer was used to perform a micro-analysis (% C, H, and N). FT-IR spectra were recorded using KBr pellets in the range 4000–400 cm−1 on a Bruker ALPHA FT-IR spectrophotometer. Electronic spectra in the range of 200–1100 nm were acquired using 1 cm quartz micro cuvettes on a Perkin Elmer Lambda–45 spectrophotometer. The mass spectra were recorded on Q-TOF 6000 ESI mass spectrometer. The concentration of complexes was taken at around 0.1 mM and the supporting electrolyte (TBAP) was at 0.1 M.
6
Comparative Analysis of Laccases and Transglutaminase
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Low redox Melanocarpus albomyces laccase (MaL, pH-range 5.0–7.5) was overproduced in Trichoderma reesei. High redox Trametes hirsuta laccase (ThL, pH-range 4.5–5.0) was produced in its native host following chromatographic purification [46 (link),47 (link)]. The reactivities of the enzyme preparations were determined against 2.2-azinobis-(3-ethylbenzothiazoline)-6-sulfonate (ABTS) at pH 4.5 in 25 mM Na-succinate buffer [46 (link)] using Perkin Elmer Lambda 45 spectrophotometer (USA) at 436 nm (ε = 29.300 M−1 cm−1). For ThL (3.5 mg mL−1), the activity was 5270 nkat mL−1 and, for MaL (8.1 mg mL−1), it was 2050 nkat mL−1. Tgase (pH-range 4–9) [17 (link)] was purchased from Activa MP Ajinomoto (Japan). After further purification, the enzyme activity (8764 nkat mL−1) was determined as previously described [48 (link)].
7
UV-Vis-NIR Absorption of SP Solutions
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UV–vis–NIR absorption spectra were recorded with a PerkinElmer LAMBDA 45 spectrophotometer. For the measurements (270–1000 nm), 3 mg of SP in 2 mL DCM solutions were placed in optical glass macrocuvette (10 mm light path). The MC spectrum was recorded after the optical stimulation of the solution by means of an external UV light source.
8
Characterization of Sorafenib-loaded Nanoparticles
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The UV–vis
spectra were recorded with a PerkinElmer Lambda
45 spectrophotometer. The fluorescence spectra were recorded with
a PerkinElmer LS55 spectrofluorimeter. All of the samples were placed
in a quartz cuvette with 1 cm optical path length. Hydrodynamic diameters
and size distributions of PluS NPs, Sorafenib-loaded PluS NPs (SRF-PluS
NPs), and SRF-F127 micelles were determined using dynamic light scattering
(DLS). DLS measurements were carried out using a Malvern Zetasizer
Nanoseries equipped with a 633 nm laser. All DLS measurements were
performed in PBS (pH 7.4) at 25 °C and at a scattering angle
of 173°. For each sample, mean hydrodynamic sizes and polydispersity
index (PDI) were determined from three measurements of the autocorrelation
function using cumulant analysis. Reported mean hydrodynamic diameters
for each condition were determined by averaging values from triplicate
measurements. Errors on mean hydrodynamic diameters were calculated
from the standard deviation (SD) of values obtained from triplicate
measurements.
spectra were recorded with a PerkinElmer Lambda
45 spectrophotometer. The fluorescence spectra were recorded with
a PerkinElmer LS55 spectrofluorimeter. All of the samples were placed
in a quartz cuvette with 1 cm optical path length. Hydrodynamic diameters
and size distributions of PluS NPs, Sorafenib-loaded PluS NPs (SRF-PluS
NPs), and SRF-F127 micelles were determined using dynamic light scattering
(DLS). DLS measurements were carried out using a Malvern Zetasizer
Nanoseries equipped with a 633 nm laser. All DLS measurements were
performed in PBS (pH 7.4) at 25 °C and at a scattering angle
of 173°. For each sample, mean hydrodynamic sizes and polydispersity
index (PDI) were determined from three measurements of the autocorrelation
function using cumulant analysis. Reported mean hydrodynamic diameters
for each condition were determined by averaging values from triplicate
measurements. Errors on mean hydrodynamic diameters were calculated
from the standard deviation (SD) of values obtained from triplicate
measurements.
9
Enzymatic Assay of Recombinant PfNDH2 Protein
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Recombinant PfNDH2 protein was expressed and purified as described in previous study10 (link). The enzymatic activity of PfNDH2 proteins was measured spectrophotometrically using NADH and ubiquinone-1 (UQ1) as substrates. Standard assays were carried out at 25 °C in 1.6 mL of reaction mixture containing 50 mmol/L MOPS buffer, pH 7.0, 150 mmol/L NaCl, 1 mmol/L EDTA, 0.01% Triton-X-100, 200 μmol/L NADH, 100 μmol/L UQ1, 0.5 nmol/L enzymes, and selected concentrations of inhibitors. Reactions were initiated by the enzyme addition. Progress of the reaction was monitored continuously by following the decrease of signal from NADH at 340 nm, in a Lambda 45 spectrophotometer (PerkinElmer Life Sciences) equipped with a magnetic stirrer in the cuvette holder. Activities were calculated using an NADH extinction of 6220 L/(mol·cm) at 340 nm. IC50 values were determined by nonlinear regression analysis of logistic concentration (GraphPad Prism software). In the enzyme kinetic studies, different concentrations of substrates were used (UQ1: 5, 10, 20, 30, 40, 60, 80, 100 μmol/L. NADH: 10, 20, 30, 50, 75, 100, 200, 600 μmol/L).
10
Spectrophotometric Titration of Copper(II)
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All reagents and solvents were used as received (from Aldrich, St. Louis, MO, USA) without further purification: copper(II) sulphate hydrate (≥98%), 3-(N-Morpholino)propanesulfonic acid (MOPS, ≥99.5%), sodium hydroxide (≥98%), N,N-dimethylformamide (spectroscopic grade, DMF). A Milli-Q system (Millipore, Billerica, MA, USA) was used for the purification of water (resistivity ≥18.2 MΩ). MOPS bufferstock solution were obtained by a dissolution in Milli-Q water of 3-(N-morpholino)propane sulphonic acid to a final concentration of 10−3 M. The pH was corrected with a solution of sodium hydroxide 1 N to a value of pH 7.4. Absorption spectra were recorded on a Perkin-Elmer Lambda 45 spectrophotometer at room temperature. Spectrophotometric titrations were performed as follows: stock solutions of ligands (ca. 10−3 M) were prepared in DMF, diluted down to the desired concentration, in the quartz cuvette, in MOPS buffer 10−3 M pH 7.4/DMF (1:4) to a final volume of 2.5 mL and then titrated by adding increasing amounts of Cu(II) (3.04 × 10−3 Min DMF).
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