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Lambda 35 uv vis

Manufactured by PerkinElmer
Sourced in United States

The Lambda 35 UV/VIS is a high-performance dual-beam spectrophotometer designed for a variety of applications in laboratory settings. It features a wavelength range of 190 to 1100 nanometers and provides accurate and reliable measurements of absorbance, transmittance, and reflectance. The instrument is equipped with a tungsten-halogen and deuterium lamp for optimal coverage of the UV and visible light spectrum.

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26 protocols using lambda 35 uv vis

1

Characterization of Zn-Al Layered Double Hydroxides

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XRD patterns of the samples were recorded with the DRON-4-07 diffractometer (CuKα radiation). Calculation of apparent crystallite size for LDHs has been performed by Debye-Scherrer formula: β(2θ) = 0.94λ/(Dcos θ°), using (003) and (110) reflection, employing the FWHM procedure. The thermogravimetric analysis (TGA) and differential thermal analysis (DTA) were carried out using Derivatograph Q-1500 D MOM (Hungary) equipment operated under a flow of an air at the heating rate of 10° min−1. Infrared spectra were obtained in the range of 4000–400 cm−1 on a Thermo Nicolet NEXUS FT-IR spectrophotometer (Nicollet, USA). The morphology and microstructure of Zn-Al LDHs were examined by the scanning electron microscope (SEM; JSM-6490-LV, JEOL, Japan). Diffuse reflectance spectra were obtained with a Lambda 35 UV–Vis (Perkin Elmer) spectrometer equipped integrated with Labsphere RSA-PR-20 in the range of wavelength 200–1000 nm. The UV–visible spectra of the solutions were recorded on a Lambda 35 UV–Vis (Perkin Elmer) spectrometer using a quartz cell (1-cm path length), with distilled water as a blank.
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2

Determination of Total Phenolic Content

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The total phenolic content was determined by Folin-Ciocalteu colorimetric method with some modifications [22 (link)]. For the analyses, aliquots of 100 μL of the samples and standard solutions were transferred to test tubes, where 500 μL of Folin-Ciocalteu reagent and 6 mL of distilled water were added. Then, they were agitated and left at rest for 1 minute. After alkalizing the medium, 2 mL of Na2CO3 solution 15% was added, and the volume was completed to 10 mL with distilled water. After 30 minutes at room temperature and being protected from light, samples were analysed in a spectrophotometer Perkin Elmer UV-VIS Lambda 35 (Norwalk, CT, USA) at 750 nm. The total phenolic content was expressed in milligrams of gallic acid equivalent per mL of sample (mgGAE/mL).
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3

Determination of Total Phenolic Content

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The Folin-Ciocalteu colorimetric method with some modifications was used to determine the total phenolic content [19 ]. To a test tube were added 100 μL of the sample, 500 μL of Folin-Ciocalteu, and 6 mL of water; the tube was agitated and left to rest for one minute. Two milliliters of Na2CO3 solution 15% was added after alkalizing the medium, and the volume was completed to 10 mL with distilled water. It was read in a spectrophotometer Perkin Elmer UV-VIS Lambda 35® (Norwalk, CT, USA) at a wavelength of 750 nm after 30 minutes at room temperature and protected from light. The total phenolic content was expressed in milligrams of gallic acid equivalent per mL of sample (mgGAE/mL).
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4

UV-Vis Spectroscopy of PVT Nanocomposites

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The UV-Vis spectra of 0.025% water solutions of PVT and the nanocomposites were recorded relative to distilled water in a 1 cm quartz cell on a Perkin Elmer LAMBDA 35 UV-Vis spectrophotometer (Waltham, MA, USA) in the wavelength range of 200–700 nm.
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5

Absorption Spectra of Graphene Oxide

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Absorption spectra in the range of 200–850 nm for GOn, G-P-123, and P-123 (only) were obtained using a spectrophotometer (Lambda 35 UV/Vis, Perkin-Elmer, MA, USA). Samples at 25 µg mL−1 concentration were analyzed in a 50 µL quartz cuvette (Hellma Analytics, Müllheim, Germany) with 10 mm light path length. All measurements were subjected to baseline correction using water as a blank control at room temperature.
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6

Fibrillation of Fibronectin and Fibrinogen Proteins

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Protein stock solutions of FN (Chemicon, Limburg an der Lahn, Germany) and FG (Calbiochem, Merck, Darmstadt, Germany) were prepared by dissolving the proteins in ultrapure water at 37 °C. The initial concentration was determined by UV-Vis spectroscopy (LAMBDA 35 UV/Vis, PerkinElmer, Waltham, USA) and further adjusted to concentrations of 20 ng μl−1 for each solution. In the next step, the stock solution of FN and FG were mixed to obtain protein solutions with the molar protein ratios shown in Table 1. After that, ethanol was added until an ethanol concentration of 80 vol% was reached. The ethanol/protein mixtures were incubated in a water bath at 37 °C for 4 hours. We chose these parameters after we tried to find self-assembly conditions to obtain reproducible fibers of FN and FG, based on our previous experience.27 (link) Finally, 20 μl of the fiber dispersion was drop-cast onto cleaned PS. The coated substrates were dried in a vacuum. After drying, the protein nanofibers' morphology was investigated by AFM.
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7

Spectrophotometric Color Analysis

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CIE (Commission Internationale de l’Eclairage) L*, a* and b* color coordinates were measured [57 ,58 ]. Visible spectra were recorded at 400–700 nm transmittance using a spectrophotometer Lambda 35 UV⁄Vis (PerkinElmer) equipped with the RSA-PE-20 Integrating Sphere accessory assembly (Labsphere, North Sutton, NH, USA). UV WinLab Software was used to record the spectra (version 2.85.04, PerkinElmer Inc.) and CIE L*a*b* color coordinates were calculated for the CIE illuminant D65 and 10° standard observed conditions, using Color software (version 3.00, 2001, PerkinElmer Inc.). Samples transmittance was measured using a 1 mm quartz cuvette.
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8

Spectroscopic Analysis of CR Fibrils

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Spectra were recorded at room temperature, using a Lambda 35 UV/VIS spectrometer (PerkinElmer). Samples contained 10 µM CR, 50 mM Tris buffer (pH 8.0) and 20 µM fibrils and were incubated for 2 min before measurement. Absorption spectra were recorded from 300 to 700 nm using a slit width of 1 nm and a scan speed of 480 nm/min.
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9

Peach Polyphenol Oxidase Extraction and Activity

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The extraction of polyphenol oxidase (PPO) from peach puree and analysis of PPO activity were performed according to the method described by Baltacıoğlu and Coruk (2021) with small modifications. Briefly, 3 g of peach puree was homogenized with 10 mL phosphate buffer (0.1 M, pH 6.5, containing 5% poly(vinylpolypyrrolidone) (PVPP)), and the mixture was centrifuged at 5525 g at 4 °C for 15 min (4 K15, Sigma, Germany). The supernatant was collected and the crude extract was kept at 4 °C before analysis. The assay mixture consisted of 3 mL 0.1 M pyrocatechol dissolved in 0.1 M phosphate buffer and 0.5 mL crude extract. The absorbance change at 420 nm at 25 °C was recorded for 1 min using a UV-VIS spectrometer (Lambda 35 UV/VIS, PerkinElmer, USA). An enzyme activity unit was defined as an increase of 0.1 in absorbance at 420 nm per min. The residual activity (RA) was defined as: Residual activity (%)=specific activity after treatmentspecific activity before treatemnt×100
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10

Bacterial Cultivation and Antibiotic Selection

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Strains and plasmids used in this study were listed in Table 1. A. avenae subsp. avenae strains were grown in Luria-Bertani (LB) broth or LB with 1.5% (w/v) agar at 30°C. LB agar without sucrose and LB agar containing 10% (w/v) sucrose were used for deletion mutagenesis (Li et al., 2011 (link)). The bacterial optical density (OD600) was determined with a spectrophotometer (Perkin Elmer Lambda35 UV/VIS). When required, antibiotics were added at the following concentrations: ampicillin (Amp), 100 μg ml-1; chloromycetin (Chl), 3.4 μg ml-1; kanamycin (Km), 50 μg ml-1; and rifampicin (Rif), 100 μg ml-1.
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