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Uv 2101 spectrophotometer

Manufactured by Shimadzu
Sourced in Japan

The Shimadzu UV-2101 is a double-beam spectrophotometer designed for accurate absorption measurements in the ultraviolet and visible wavelength ranges. It features a high-performance monochromator and a photomultiplier detector to provide precise and reliable data.

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5 protocols using uv 2101 spectrophotometer

1

Spectrophotometric Analysis of Myoglobin Redox Forms

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Control and glycoconjugated samples were diluted to 1 mg/mL with 50 mM potassium phosphate buffer (pH 7.4) and the absorption was recorded at 557, 582, 503 and 525 nm using a Shimadzu UV-2101 spectrophotometer (Kyoto, Japan) with cuvettes of 1 cm path length. The relative proportions of the myoglobin redox forms: deoxymyoglobin (DeoMb), oxymyoglobin (OxyMb) and metmyoglobin (MetMb) were calculated according to the modified Krzywicki’s equation described by Tang et al. [16 ] as follows:
[DeoMb]  =  - 0.543R1+ 1.594R2+ 0.552R3 1.329
[OxyMb]   =  0.722R1 1.432R2 1.659R3+ 2.599
[MetMb]  =  - 0.159R1 0.085R2+ 1.262R3 0.520
where R1 = A582/A525, R2 = A557/A525 and R3 = A503/A525.
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2

Direct and Coupled Assays for MAO-A

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The direct spectrophotometric assay using purified MAO-A (30–50 nM) was added last to a 1 mL final volume of 50 mM potassium phosphate pH 7.5 containing inhibitor (0–100 μM) and 0.3 mM kynuramine (equivalent to 2× KM). The increase in absorbance was followed at 314 nm in a Shimadzu UV-2101 spectrophotometer. The coupled assay [53 (link)] in black 96-well plates (Eppendorf UK Ltd., Stevenage, UK) used tyramine, Ampliflu™ Red (AR), horseradish peroxidase (HRP) and membrane-bound human MAO-A and MAO-B purchased from Sigma-Aldrich (Dorset, UK). Final concentrations were 50 μM AR, 1 U/mL HRP, and 1 nM enzyme. The substrate was tyramine either at 2× KM (0.8 mM for MAO-A or 0.32 mM for MAO-B) for reversible binding or at 1 mM to assess remaining active MAO after incubation with the inactivators.
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3

Synthesis and Characterization of Triazenes

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All chemicals and anhydrous solvents were purchased from Sigma-Aldrich, Merck, Alfa Aesar and TCI and used without further purification. Melting points (mp) were determined with SMP30 melting point apparatus in open capillaries and are uncorrected. FT-IR spectra were recorded by using Perkin Elmer Spectrum 100 FT-IR spectrometer. Ultraviolet–visible (UV–vis) absorption spectra were recorded on Shimadzu UV-2101 spectrophotometer in DMSO. Nuclear Magnetic Resonance (1H-NMR and 13C-NMR) spectra of compounds were recorded using a Bruker Advance III 300 MHz spectrometer in DMSO-d6 and TMS as an internal standard operating at 300 MHz for 1H-NMR and 75 MHz for 13 C-NMR. Thin layer chromatography (TLC) was carried out on Merck silica gel 60 F254 plates.
The ligands 3–(3-(4-fluorophenyl)triaz-1-en-1-yl) benzenesulfonamide (L1), 3–(3-(4-methoxyphenyl)triaz-1-en-1-yl) (L2), benzenesulfonamide 4–(3–(3-sulfamoylphenyl)triaz-2-en-1-yl) benzoic acide (L3), 3–(3-(3,4-dimethoxyphenyl)triaz-1-en-1-yl) benzenesulfonamide (L4), and 3-(3-(3,5-dimethylphenyl)triaz-1-en-1-yl)benzenesulfonamide (L5) were synthesised and characterised as previously described by us20 .
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4

Yeast Growth and Viability Assays

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The yeast growth was followed by periodic optical density measurement (640 nm) of the appropriately diluted culture samples in a Shimadzu UV-2101 spectrophotometer (Shimadzu, Kyoto, Japan) and by counting the colony-forming units in YPD plates after incubation at 30°C, for 48 h. Further, the yeast cell biomass was determined using 2 × 50 and 3×15 ml samples centrifuged in pre-weighed tubes for 10 min at 2300 × g, washed twice with sterile deionized water, dried for 24 h at 100°C, and stored in a desiccator before weighing.
To evaluate the viability of nitrogen-starved cells, a sample from each low-nitrogen fermentation was spread onto yeast carbon base (YCB, Difco) agar plates with 0.73 mg N l−1 as amino acids: histidine.HCl (1 mg l−1), methionine (2 mg l−1) and tryptophan (2 mg l−1). YCB was used to test the ability of yeasts to assimilate nitrogen by adding diverse nitrogen sources. The histidine, methionine and tryptophan concentrations were reduced to 10% of their original concentration in the yeast nitrogen base. This experiment was expected to detect viable cells in solid media without a nitrogen source.
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5

Comprehensive Wine Composition Analysis

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Color intensity (CI) and hue were determined by the OIV method [35 ], total polyphenol index (TPI) was determined by Curvelo-Garcia method [36 ], total phenols, non-flavonoids and flavonoids were determined according to Kramling and Singleton [37 ]. Total anthocyanins were analyzed by SO2 bleaching method, described by Ribéreau-Gayon et al., [38 ], colored anthocyanins (CA), total pigments (TP) and polymeric pigments (PP) were analyzed by the method described by Somers and Evans [39 (link)], and total tannins were determined by the LA method [40 ]. All samples were analyzed by a spectrophotometer (GENESYSTM 10 series spectrophotometers). The absorption spectra of WW samples were recorded with a Shimadzu UV-2101 spectrophotometer (Shimadzu, Kyoto, Japan) scanned from a range between 380 and 770 nm, with 5 nm distance, using 1 cm path length quartz cells. Data were collected to determine L (lightness), a (redness), and b (yellowness) coordinates using the CIELab 1976 method. This allows reliable quantification of the overall color difference of a sample when compared to a reference sample (blank). Color differences can be distinguished by the human eye when the differences between ΔEab* values are greater than two units, in accordance to Spagna et al. [41 (link)]. All analyses were performed in duplicate. Table 2 resumes the formulas used in this work.
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