Lcq ion trap mass spectrometer

Manufactured by Thermo Fisher Scientific

Sourced in United States

The LCQ ion trap mass spectrometer is a laboratory instrument designed for the detection and analysis of chemical compounds. It operates by using an ion trap to capture and analyze ionized molecules, providing detailed information about their molecular structure and composition.

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Lab products found in correlation

Atlantis t3 c18 column, by Waters Corporation (1 mentions) Avance 500 mhz nmr spectrometer, by Bruker (1 mentions) Spd m20a, by Shimadzu (1 mentions) Kinetex pfp column, by Phenomenex (1 mentions) Prominence system, by Shimadzu (1 mentions) Drx 500, by Bruker (1 mentions) Xcalibur software, by Thermo Fisher Scientific (1 mentions) Merck 60 f254, by Merck Group (1 mentions) Q exactive hybrid quadrupole orbitrap mass spectrometer, by Thermo Fisher Scientific (1 mentions) Vxr 300 spectrometer, by Agilent Technologies (1 mentions) P 2000 polarimeter, by Jasco (1 mentions) Ltq orbitrap xl hybrid ion trap orbitrap mass spectrometer, by Thermo Fisher Scientific (1 mentions) Avance 3 500 ft nmr spectrometer, by Bruker (1 mentions) Lc 20a, by Shimadzu (1 mentions) Shim pack vp ods c18 column, by Shimadzu (1 mentions) 400 mhz nmr spectrometer, by Agilent Technologies (1 mentions) Deuterated solvent, by Merck Group (1 mentions) Cos 1, by National Centre for Cell Science (1 mentions) Cleancap egfp mrna, by TriLink (1 mentions) Hek 293, by National Centre for Cell Science (1 mentions)

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15 protocols using lcq ion trap mass spectrometer

Purification and Identification of LEGCG

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Waters HPLC systems comprise a 1525 pump and a 2998 diode array detector (DAD) was used for analysis. The separation was performed by a 5 μm Waters Atlantis T3-C18 column (250 × 4.6 mm). The mobile phase was 0.1% acetic acid (A) and methanol (B) with a gradient program of 0−30 min, 40%−100% B linear gradient elution. The injection volume was 20 μL and the flow rate was 1 mL/min. The detection wavelength was set at 280 nm. A Thermo Scientific LCQ Ion-Trap Mass Spectrometer (Thermo Fisher Scientific, San Jose, CA, USA) with electrospray ionization (ESI) at positive mode was used for the HPLC-MS/MS analysis. The conditions were: Dry gas flow, 35 L/min; capillary voltage, 3.5 kV; nebulizer, 30 psi; collision energy, 16 eV; desolvation temperature, 400 °C.
To get purified LEGCG, Waters semi-preparative HPLC systems comprise a 600E pump and a 2998 DAD was used. The separation was carried out using a 19 mm Waters Atlantis OBD-C18 column (10 μm, 250 mm). The mobile phases were 0.1% acetic acid (A) and methanol (B). The gradient program was 0−30 min, 40%−100% B linear gradient elution, at a flow rate of 5 mL/min. The injection volume was 100 μL. The UV absorbance was detected at 280 nm. A Bruker Avance 500 MHz NMR spectrometer (Bruker Biospin GmbH, Rheinstetten, Germany) was carried out for the purified LEGCG to identify its molecular structure.

Chen J., Zhang L., Li C., Chen R., Liu C, & Chen M. (2019). Lipophilized Epigallocatechin Gallate Derivative Exerts Anti-Proliferation Efficacy through Induction of Cell Cycle Arrest and Apoptosis on DU145 Human Prostate Cancer Cells. Nutrients, 12(1), 92.

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HPLC Analysis of CoA Esters

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CoA esters were analyzed by HPLC using a Kinetex PFP column (5 mm, 100 A°, 250 3 4.6 mm; Phenomenex, USA) on a Shimadzu Prominence system with PDA detector (SPD-M20A). The temperature was set to 40 °C and a flow rate of 0.75 mL min^− 1 was used. The injection volume was 5 μL. 100 mM ammonium acetate (eluent B) and acetonitrile (eluent A) were used as eluents. The separation started with 5% eluent A for 15 min followed by a gradient step (1 min) up to 80% eluent A, holding 80% eluent A for 1 min, an additional gradient (1 min) back to 5% eluent A and a re-equilibration with 5% eluent A for 8 min. For HPLC-electrospray ionization (ESI)-MS/MS, an Agilent 1100 HPLC system and the Kinetex PFP column (see above) connected to an LCQ ion trap mass spectrometer (Thermo Fisher Scientific) was used [30 (link)]. The injection volume was 50 μL. The column was run isocratically with 95% 100 mM ammonium acetate and 5% acetonitrile for 10 min at a flow rate of 0.75 ml/min and a temperature of 40 °C.

Frey J., Kaßner S., Spiteller D., Mergelsberg M., Boll M., Schleheck D, & Schink B. (2021). Activation of short-chain ketones and isopropanol in sulfate-reducing bacteria. BMC Microbiology, 21, 50.

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Characterization of HL-60 Cell O-Glycome

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HL-60 O-glycan structures were measured using the Cellular O-glycome Reporter (CORA) method described recently32 (link). Here, 50–80 μM per-acetylated Benzyl-α-GalNAc was fed to HL-60 cells plated at an initial density of 0.2 × 10⁶cells/ml in Advanced DMEM media without phenol red or serum proteins for 3 days. Benzyl-α-GalNAc derivatives were then purified from 5 mL of cell culture supernatant using the Sep-Pak C18 method described previously32 (link). Eluates obtained using 50% methanol were permethylated32 (link). Products were analyzed using an LCQ ion trap mass spectrometer (Thermo). All product structures were confirmed using MSⁿ (n = 2-4) spectral analysis.

Stolfa G., Mondal N., Zhu Y., Yu X., Buffone A J.r, & Neelamegham S. (2016). Using CRISPR-Cas9 to quantify the contributions of O-glycans, N-glycans and Glycosphingolipids to human leukocyte-endothelium adhesion. Scientific Reports, 6, 30392.

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Mass Spectrometry Analysis of Potential Antivirals

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Three potential antiviral compounds of small molecular weight (pending patent) were selected for this study and given different codes (AAHL 13, AAHL 18 and AAHL 42). The compounds were initially dissolved in methanol at a concentration of 0.5 mg/ml, then diluted in 50% methanol/0.2% formic acid to a final concentration of 10 μg/ml. Diluted samples were analysed by direct infusion at a rate of 10 μl/min into the electrospray ionisation source of an LCQ ion-trap mass spectrometer (Thermo, San Jose, CA, USA). Spectra were acquired and averaged over 50 consecutive scans. Full scans were acquired over the mass range m/z 50–500 to give an indication of sample purity. High resolution zoom scans were also performed that allowed determination of the mass/charge state of the selected ion and hence an accurate mass measurement of the selected ion.

Alshammari T.M., Al-Hassan A.A., Hadda T.B, & Aljofan M. (2015). Comparison of different serum sample extraction methods and their suitability for mass spectrometry analysis. Saudi Pharmaceutical Journal : SPJ, 23(6), 689-697.

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Synthesis and Characterization of C-L Peptide

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The C-L peptide (KWKLFKKIFKRIVQRIKDFLRN) was chemically synthesized (95% purity) by KangLong Biochemistry (Jiangsu, China). The molecular weight of the C-L peptide was confirmed using a Thermo Finnigan LCQ ion-trap mass spectrometer (Thermo Finnigan, CA, USA). The peptide was then suspended in endotoxin-free water and stored at −80°C.

Wei X., Zhang L., Zhang R., Koci M., Si D., Ahmad B., Cheng J., Wang J., Aihemaiti M, & Zhang M. (2020). A Novel Cecropin-LL37 Hybrid Peptide Protects Mice Against EHEC Infection-Mediated Changes in Gut Microbiota, Intestinal Inflammation, and Impairment of Mucosal Barrier Functions. Frontiers in Immunology, 11, 1361.

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Characterization of Organic Compounds

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All reactions were performed under N₂ unless otherwise noted. All ¹H NMR and ¹³C NMR were recorded at 500 and 125 MHz, respectively, on a Bruker DRX 500. Chemical shifts were referred to TMS as internal standard in the case of CDCl₃ solution and to the residual proton signal of DMSO at 2.5 ppm in the case of DMSO-d₆ solution. The following abbreviations were used in reporting spectra: s=singlet, d=doublet, t=triplet, m=multiplet. Mass spectra were recorded on a Thermo Fisher LCQ ion trap mass spectrometer. High-resolution mass spectra (HRMS) were obtained using a Bruker Apex ion cyclotran resonance mass spectrometer in ESI positive mode. Unless otherwise mentioned, all of the solvents used were of laboratory reagent grade. Usually, the flash chromatography was performed using 100–200 mesh silica gel. All of the organic extracts were dried over sodium sulfate after work up. For analytical reversed-phase HPLC a Vydac 218-TP54 column (5 _ 250 mm) was used with a l gradient of 10–90% acetonitrile in 0.1% TFA/H₂O over 40 min at a flow rate of 1 mL/min.

Deekonda S., Wugalter L., Kulkarni V., Rankin D., Largent-Milnes T.M., Davis P., Bassirirad N.M., Lai J., Vanderah T.W., Porreca F, & Hruby V.J. (2015). Discovery of 5-Substituted Tetrahydronaphthalen-2yl) methyl with N-phenyl-N-(piperidin-4-yl)propionamide Derivatives as Potent Opioid Receptor Ligands. Bioorganic & medicinal chemistry, 23(18), 6185-6194.

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Quantitative Analysis of Plant Compounds

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Quantitations were done by connecting the same column with the same elution program to a SpectraSystem equipped with an AS3000 autosampler and a P4000 quaternary pump. The system was controlled with the Xcalibur software version 1.2 (ThermoFisher). Compounds were monitored from 200 to 800 nm with a UV6000LP diode array detector. Mass spectra were acquired with an LCQ ion trap mass spectrometer equipped with an ESI source (ThermoFisher). Collision-induced dissociation spectra were recorded at a relative collision energy of 30, 35, and 40%, respectively, for singly charged [M−H]⁻¹ ions of monomers (m/z 289), dimers (m/z 577, 575), and trimers (m/z 865, 863, 861). The ESI inlet conditions were as follows: source voltage, 4.9 kV; capillary voltage, –4 V; capillary temperature, 200 °C; sheath gas, 39 psi. Semi-quantitations were done with the calibration curves of C1 for all C1-derived compounds except catechin, epicatechin, and B2, for which their own respective calibration curves were used.

De Taeye C., Kankolongo Cibaka M.L, & Collin S. (2017). Occurrence and Antioxidant Activity of C1 Degradation Products in Cocoa. Foods, 6(3), 18.

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Tryptic Peptide Characterization of Radix Trichosanthis

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MS and MS/MS characterization and detection of the tryptic peptides derived from Radix Trichosanthis was performed using an LCQ ion-trap mass spectrometer (Thermo Inc., San Jose, California, USA) by means of electrospray ionization (ESI). A gradient elution of solvents A (water containing 0.1% FA) and B (acetonitrile with 2% water and 0.1% FA) was applied with a flow rate of 200 μl/min as follows: 0-5 min, 0% solvent B; 5-80 min, 0%-50% solvent B; 80-105 min, 50%-100% solvent B; and 105-120 min, 100% B. The nitrogen sheath and auxiliary gas flow were maintained at 20 and 5 arbitrary units, respectively. The heated capillary temperature was 300 ºC and the spray voltage was set to 5 kV in positive ion mode. The three ions with the highest intensity were subjected to MS/MS fragmentation under a normalized collision energy (NCE) of 30 and the resulting fragment ion profiles were then trawled using the Protein Discoverer 1.0 (Thermo Finnigan; San Jose, California, USA) against a customized FASTA database. Only peptides with sufficient confidence (i.e., probability > 40) were retained.

Sang M., Ying Y., Wu Q., Ma C., Xi X., Zhou M., Wang L., Bininda-Emonds O.R.P, & Chen T. (2019). Cloning of a novel trypsin inhibitor from the Traditional Chinese medicine decoction pieces, Radix Trichosanthis. Analytical biochemistry, 578.

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Quantifying Malate in Plant Leaves

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The malate concentration in the leaves of 4-week-old plants grown in soil under a 12-h light/12-h dark cycle was determined as follows. The unfolded leaves were taken at each specified time point, immediately frozen in liquid nitrogen, and stored at À80 C until analysis. Each sample was extracted by rapidly grinding it in liquid nitrogen and then adding distilled water. The malate concentration in the extract was determined by high-performance liquid chromatography electrospray ionization mass spectrometry (using a 4000 QTRAP instrument; AB Sciex, Framingham, MA, USA). The liquid chromatography system was equipped with an Aminex HPX-87H column (300 mm long, 7.8 mm internal diameter, 9 mm particle size; Bio-Rad Laboratories, Hercules, CA, USA) connected to an LCQ ion trap mass spectrometer (Thermo Fisher Scientific). The mobile phase was 1% formic acid in water, and an analytical run lasted 26 min, with a mobile phase flow rate of 400 ml min À1 . The target compounds were analyzed using appropriate multiple reactions for monitoring ion pairs.

Dong H., Bai L., Zhang Y., Zhang G., Mao Y., Min L., Xiang F., Qian D., Zhu X, & Song C.P. (2018). Modulation of Guard Cell Turgor and Drought Tolerance by a Peroxisomal Acetate-Malate Shunt. Molecular plant, 11(10).

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Analytical Characterization of Organic Compounds

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All reagents and solvents, unless differently stated, were used as received from Sigma Aldrich (St. Louis, MO, USA). Chromatography was performed on silica gel (Merck 60, 70–230 mesh); homogeneity was confirmed by TLC on silica gel Merck 60 F₂₅₄ (Sigma Aldrich, St. Louis, MO, USA). ¹H- and ¹³C-NMR spectra were recorded on a Varian VXR-300 spectrometer (Varian Inc., Palo Alto, CA, USA). The LC-MS/MS system used consisted of an LCQ ion trap mass spectrometer (Thermo Finnigan, San Jose, CA, USA) equipped with an electrospray ionization (ESI) source. HR-MS spectra were recorded using Q Exactive™ Hybrid Quadrupole-Orbitrap™ Mass Spectrometer (Thermo Fischer Scientific, Waltham, MA, USA) coupled with HPLC Dionex series Ultimate 3000 (Thermo Fischer Scientific, Waltham, MA, USA) and a Phenomenex Luna 5µ C18 150 mm × 2 mm (P/N° 00F-4041-B0) column. Mass resolution was set at 140,000, and the scan range was from 250–750 m/z (Table S1).

Cacciatore I., Marinelli L., Fornasari E., Cerasa L.S., Eusepi P., Türkez H., Pomilio C., Reale M., D’Angelo C., Costantini E, & Di Stefano A. (2016). Novel NSAID-Derived Drugs for the Potential Treatment of Alzheimer’s Disease. International Journal of Molecular Sciences, 17(7), 1035.

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