Uv 3000

Manufactured by Shimadzu

Sourced in Japan

The UV-3000 is a high-performance UV-Vis spectrophotometer manufactured by Shimadzu. It is designed to provide accurate and reliable measurements of absorbance, transmittance, and reflectance across the ultraviolet and visible light spectrum. The instrument features a wide wavelength range, high resolution, and advanced optics for precise analysis of samples.

Automatically generated - may contain errors

Lab products found in correlation

400 mhz spectrometer, by Bruker (1 mentions) 1100 series hplc, by Agilent Technologies (1 mentions) Ltq orbitrap xl hybrid ion trap orbitrap, by Thermo Fisher Scientific (1 mentions) β carotene, by Merck Group (1 mentions)

Spelling variants of this product

UV-3000 spectrophotometer (8 citations)

11 protocols using uv 3000

Spectroscopic Analysis and Chiral HPLC Characterization

Check if the same lab product or an alternative is used in the 5 most similar protocols

¹H NMR and ¹³C NMR were recorded on a Bruker-400
MHz spectrometer (¹H NMR: 400 MHz; ¹³C NMR:
100 MHz) using TMS as an internal
reference. The chemical shifts (δ) and coupling constants (J) were expressed in ppm and Hz, respectively. UV–Vis
spectrophotometry was carried out on a Shimadzu UV-3000. HPLC analysis
was carried out on an Agilent 1100 series HPLC with a multiple wavelength
detector. Chiralpak AS-H, AD-H, and OD-H columns were purchased from
Daicel Chemical Industries, Ltd. Optical rotations were measured on
a PerkinElmer polarimeter (model 343). HRMS (ESI) was recorded on
Waters Q-TOF Premier and Thermo Scientific LTQ Orbitrap XL Hybrid
Ion Trap-Orbitrap mass spectrometers. Commercially available compounds
were used without further purification. Solvents were purified according
to the standard procedures, unless otherwise noted. Commercial pyrrole
should be distilled for the use of the reactions. Ligands^{9d ,10b} and various 2-enoyl-pyridine N-oxides 2(11 (link)) were prepared according to literature
procedures.

Sun J., Gui Y., Huang Y., Li J., Zha Z., Yang Y, & Wang Z. (2020). Lewis Acid-Catalyzed Enantioselective Friedel–Crafts Alkylation of Pyrrole in Water. ACS Omega, 5(21), 11962-11970.

+ Open protocol

+ Expand

Cholinesterase Activity Assay Using Ellman's Method

Check if the same lab product or an alternative is used in the 5 most similar protocols

Cholinesterase activity was determined following the method of Ellman et al. (1961) (link). The assay was carried out in the following steps: For each sample, two tubes containing 4 ml substrate solution [20 mN Tris buffer at pH 8.2 with 20 mM magnesium chloride (MgCl₂) and 100 mM NaCl, 0.001 M Dithio-2-nitrobenzoic acid (DTNB) as reagent], and 0.001 M acetylcholine iodide, as substrate, were pre-incubated at 37 °C in a water bath for 10 min. Into each tube, 20 μl of cell culture was added. The sample was vortexed and transferred into a cuvette for absorption rating. Absorption reading was taken at one-minute time intervals for 3 min using a spectrophotometer (Shimadzu UV-3000; Shimadzu Corporation; Kyoto, Japan) at 412 nm. A substrate free blank was run in parallel with each sample tested.

Salama M., Lotfy A., Fathy K., Makar M., El-emam M., El-gamal A., El-gamal M., Badawy A., Mohamed W.M, & Sobh M. (2015). Developmental neurotoxic effects of Malathion on 3D neurosphere system. Applied & Translational Genomics, 7, 13-18.

+ Open protocol

+ Expand

Bovine Heart Mitochondrial Complex I Assay

Check if the same lab product or an alternative is used in the 5 most similar protocols

SMPs were prepared from isolated bovine heart mitochondria by the method of Matsuno-Yagi and Hatefi (54 ) and stored in buffer containing 0.25 M sucrose and 10 mM Tris–HCl (pH 7.4) at −80 °C until use. NADH-UQ oxidoreductase activity in SMPs was measured spectrophotometrically by following the oxidation of NADH with a Shimadzu UV-3000 instrument (340 nm, ε = 6.2 mM⁻¹ cm⁻¹) at 30 °C (25 (link)). The reaction medium (2.5 ml) contained 0.25 M sucrose, 1.0 mM MgCl₂, 0.80 μM antimycin A, 4.0 mM KCN, and 50 mM phosphate buffer (pH 7.4). The final SMP protein concentration was 60 μg of protein/ml. The reaction was initiated by adding 50 μM NADH after the equilibration of SMPs with UQ (and an inhibitor if necessary) for 4 min.
The content of complex I in SMPs was roughly estimated as the minimal amount of bullatacin (a very potent inhibitor of bovine complex I) needed to completely inhibit the NADH oxidase activity because this inhibitor binds to the enzyme in an almost stoichiometric manner (55 (link)). The content of complex I in 1.0 mg of SMP protein was estimated to be 0.10 nmol (55 (link)).

Uno S., Masuya T., Zdorevskyi O., Ikunishi R., Shinzawa-Itoh K., Lasham J., Sharma V., Murai M, & Miyoshi H. (2022). Diverse reaction behaviors of artificial ubiquinones in mitochondrial respiratory complex I. The Journal of Biological Chemistry, 298(7), 102075.

+ Open protocol

+ Expand

Purification and Enzymatic Assay of Complex I

Check if the same lab product or an alternative is used in the 5 most similar protocols

Complex I was purified from bovine heart mitochondria by solubilization with sodium deoxycholate and n-decyl-β-d-maltoside, and purified by sucrose density gradient centrifugation and anion-exchange chromatography, as described previously (56 (link)). NADH-UQ oxidoreductase activity with the isolated complex I was measured spectrophotometrically by following the oxidation of NADH with a Shimadzu UV-3000 instrument (340 nm, ε = 6.2 mM⁻¹ cm⁻¹) at 30 ˚C (25 (link)). The reaction medium contained 0.40 mg/ml asolectin, 0.08% CHAPS, and 20 mM Tris–HCl buffer (pH 7.5). The final enzyme concentration was 7.5 μg of protein/ml (7.5 nM). The reaction was initiated by adding 50 μM NADH after the equilibration of the enzyme with UQ (and an inhibitor if necessary) for 4 min.

+ Open protocol

+ Expand

Measuring NADH-UQ1 Oxidoreductase Activity

Check if the same lab product or an alternative is used in the 5 most similar protocols

The NADH-UQ₁ oxidoreductase activity of purified Na⁺-NQR was determined by following reduction of UQ₁ at 282 nm (ε₌ 14.5 mM^{− 1} cm^{− 1}) with a Shimadzu UV-3000 instrument at 30 °C [16 (link)]. The reaction medium (2.5 ml) contained 5% glycerol, 0.05% DDM, 1 mM EDTA, 100 mM NaCl, and 50 mM Tris-HCl (pH 8.0). The final enzyme concentration was set to 0.90 nM. The reaction was started by the addition of 100 μM NADH after the incubation of the enzyme with UQ₁ for 1 min. When the effects of inhibitors were examined, the enzyme was incubated with inhibitor for 1 min before the addition of UQ₁.

Ishikawa M., Masuya T., Tanaka H., Aoki W., Hantman N., Butler N.L., Murai M., Barquera B, & Miyoshi H. (2021). Specific chemical modification explores dynamic structure of the NqrB subunit in Na+-pumping NADH-ubiquinone oxidoreductase from Vibrio cholerae. Biochimica et biophysica acta. Bioenergetics, 1862(8), 148432.

+ Open protocol

+ Expand

Mitochondrial ADP-Uptake and ATP-Release Assay

Check if the same lab product or an alternative is used in the 5 most similar protocols

The measurement of ADP-uptake/ATP-release in isolated yeast mitochondria was conducted according to the procedures as described previously (Unten et al., 2019 (link)). Freshly prepared mitochondria (50 μg of proteins/ml) were suspended in 2.5 ml of reaction buffer (0.60 M mannitol, 0.10 mM EGTA, 2.0 mM MgCl₂, 10 mM KP_i, 5.0 mM α-ketoglutarate, and 10 mM Tris-HCl, pH 7.4) at 30°C in the presence of an ATP-detecting system (2.5 mM glucose, hexokinase [1.7 Enzyme Units (EU)], glucose-6-phosphate dehydrogenase (0.85 EU), 0.20 mM NADP⁺, and 10 μM Ap₅A [a specific inhibitor of mitochondrial adenylate kinase]). Externally added ADP (100 μM) started the exchange reaction with ATP synthesized in the mitochondrial matrix. The formation of NADPH, which is proportional to ATP efflux, was monitored spectrophotometrically for 10 min at 340 nm (ɛ = 6.2 mM⁻¹ cm⁻¹) with a Shimadzu UV-3000 (Shimadzu Co., Kyoto, Japan).

Sakai K., Unten Y., Kimishima A., Nonaka K., Chinen T., Sakai K., Usui T., Shiomi K., Iwatsuki M., Murai M., Miyoshi H., Asami Y, & Ōmura S. (2021). Traminines A and B, produced by Fusarium concentricum, inhibit oxidative phosphorylation in Saccharomyces cerevisiae mitochondria. Journal of Industrial Microbiology & Biotechnology, 48(9-10), kuab051.

+ Open protocol

+ Expand

Spectrophotometric Heme-Binding Assay of Ssr1698

Check if the same lab product or an alternative is used in the 5 most similar protocols

The heme-binding ability of tag-less Ssr1698 was estimated by optical titrations in PBS buffer (pH 7.4) as described previously^{27 (link),28 (link)} using ultraviolet–visible spectrophotometer (UV3000, Shimadzu, Kyoto, Japan) at room temperature. To exclude the possibility of nonspecific binding of heme, the binding reactions were conducted in the presence of 20 µM BSA. For the c-type heme-binding assay, MP-11 in 1 µM increments was added to both the sample and the reference cuvettes, the former of which contained 10 µM tag-less Ssr1698 and 20 µM BSA, and the latter of which contained 20 µM BSA and not tag-less Ssr1698. For the b-type heme-binding assay, hemin in 2 µM increments was added to both the sample and the reference cuvettes, the former of which contained 20 µM tag-less Ssr1698 and 20 µM BSA, and the latter of which contained 20 µM BSA and not tag-less Ssr1698. The difference absorption spectra were obtained by subtracting the spectrum of the reference cuvette from that of sample cuvette.

Ran Z., Du Z., Miao G., Zheng M., Luo L., Pang X., Wei L., Li D, & Ma W. (2023). Identification of a c-type heme oxygenase and its function during acclimation of cyanobacteria to nitrogen fluctuations. Communications Biology, 6, 944.

+ Open protocol

+ Expand

Determining Chlorophyll Absorption Cross-Section

Check if the same lab product or an alternative is used in the 5 most similar protocols

The average specific chlorophyll optical absorption crosssection (a*) of cells (m 2 mg -1 Chl a) was determined from in vivo absorption spectra (in the range from 400 to 750 nm) according to [27] (link), using a double-beam spectrophotometer (Shimadzu UV-3000). To minimize the impact of the light scattering effect from the cell surface, the sample cuvette was placed close to the detector window with standard white printer paper as a light diffuser placed in between.
The maximum quantum yield θ max , i.e., the ratio between the rate of oxygen evolution and light absorption under limiting light, was calculated according to the following equation [28] (link):θ max = α/ a*α and a* were expressed per Chl a.

Torzillo G., Álvarez-Gómez F., Celis-Plá P.S.M., Rearte A., Gómez-Serrano C., Silva Benavides A.M., Štěrbová K., Caporgno M., Touloupakis E., Masojídek J, & Figueroa F.L. (2023). Photosynthesis and biochemical characterization of the green alga Chlamydopodium fusiforme (Chlorophyta) grown in a thin-layer cascade. Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology, 22(9).

+ Open protocol

+ Expand

NADH-driven Membrane Potential Dynamics

Check if the same lab product or an alternative is used in the 5 most similar protocols

Membrane potential formation coupled with NADH-UQ oxidoreduction in SMPs was measured by following changes in the absorbance of oxonol VI (601–630 nm) with a Shimadzu UV-3000 instrument in dual-wavelength mode in reaction medium (2.5 ml) containing 0.25 M sucrose, 1.0 mM MgCl₂, 0.80 μM antimycin A, 4.0 mM KCN, 2.5 μM oligomycin, 0.10 μM nigericin, 1.0 μM oxonol VI, and 50 mM phosphate buffer (pH 7.4) at 30 °C (27 (link)). The final mitochondrial protein concentration was set to 60 μg of protein/ml. The reaction was initiated by adding 50 μM NADH after the equilibration of SMP with UQ for 4 min.

+ Open protocol

+ Expand

Spectrophotometric Analysis of NDH-1L

Check if the same lab product or an alternative is used in the 5 most similar protocols

The purified NDH-1LΔV complex was separated by CN-PAGE. A yellow NDH-1L band was excised from the CN gel and then was analyzed by a spectrophotometer (UV3000; Shimadzu) through positioning it into a cuvette. The full wavelength scan of β-carotene (10 µM; Sigma) is conducted as a control of its typical characteristic peaks.

Zhang C., Shuai J., Ran Z., Zhao J., Wu Z., Liao R., Wu J., Ma W, & Lei M. (2020). Structural insights into NDH-1 mediated cyclic electron transfer. Nature Communications, 11, 888.

+ 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?

Revolutionizing how scientists
search and build protocols!