After an orthogonal dansyl-labeling and label-free dual pretreatment49 (link), samples were analyzed using a QTRAP 5500 mass spectrometer (AB Sciex, Foster City, CA, USA) linked to an Ultra Performance LC system (AB Sciex). The chromatographic separation was realized on Waters ACQUITY UPLC HSS T3 Column (2.1 mm × 150 mm, 1.8 μm). MRM monitoring conditions for each compound were performed on Analyst R914.6.2 (AB Sciex). The parameters of mass spectrometer were summarized as follows: ion spray voltage, +5.5 kV; temperature, 50 °C; curtain gas, 35 psi entrance potential, 10.0 V; collision cell exit potential: 13.0 V. Data acquisition and analysis were performed on Analyst R914.6.2 software (AB Sciex).
Qtrap 5500 mass
Manufactured by AB Sciex
Sourced in United States
The QTRAP 5500 mass spectrometer is a highly sensitive and versatile instrument designed for advanced quantitative and qualitative analysis. It combines the functionalities of a triple quadrupole and a linear ion trap, providing enhanced performance for a wide range of applications in analytical chemistry.
Automatically generated - may contain errors
Lab products found in correlation
Analyst r914, by AB Sciex (1 mentions)
Acquity uplc hss t3 column, by Waters Corporation (1 mentions)
Lipidview software, by AB Sciex (1 mentions)
Acquity uplc beh c18 column, by Waters Corporation (1 mentions)
Ultrafast liquid chromatography system, by Shimadzu (1 mentions)
Nanoacquity ultraperformance lc system, by Waters Corporation (1 mentions)
Proteinpilot software, by Thermo Fisher Scientific (1 mentions)
7 protocols using qtrap 5500 mass
1
Dansyl-labeling and Label-free Dual Pretreatment for Mass Spectrometry
2
Adenine Nucleotides Extraction and LC-MS Analysis
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Adenine nucleotides were extracted from cells with perchloric acid38 (link). Relative concentrations were measured by LC-MS on a QTRAP® 5500 mass spectrometer (AB-SCIEX).
3
Lipid Profiling by Direct Infusion MS
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Lipid extracts were directly infused into the TurboVion source by a syringe pump at 10 μl/min. and analysed by QTRAP5500 mass spectrometer (ABSCIEX, Farmington, MA, USA). Multiple precursor ion and neutral loss scanning methods were used for Information Dependent Acquisition of ms/ms data to detect and quantify the lipid classes as described earlier. Mass analyser conditions in the positive ion mode are as follows: Ionization Potential: 5500 V, Declustering Potential: 120 V, Entrance Potential: 9 V, Collision cell Exit Potential: 9 V. Collision energy for the survey scan was 10 and 45 eV for Enhanced Product Ion scans. In each scan, three ions with highest intensity were chosen for dependent product ion acquisition and the detected ions were excluded for the rest of the experiment after three occurrences. Data were analysed for the identification of lipid species using LipidView software (ABSCIEX). Lipid were quantified against internal standards and normalized against protein values obtained by the Bradford assay 19 (link).
4
Adenine Nucleotides Extraction and LC-MS Analysis
5
Metabolite Quantification and Isotopic Analysis
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Metabolites were acquired and quantified on an AB SCIEX Qtrap® 5500 mass spectrometer (AB SCIEX, Framingham, MA) and processed using MultiQuant® 3.0.1 as described previously34 (link). Mass isotopomer distributions (MIDs) were acquired on the same instrument and processed using MultiQuant® 3.0.1 and PeakView® 2.235 (link).
6
LC-MS/MS Method for Eribulin and Cevipabulin
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LC-MS/MS analysis was performed on an ultrafast liquid chromatography system (Shimadzu) coupled with an AB SCIEX Qtrap 5500 mass spectrometer, equipped with ESI source. Instrument control and collection of chromatographic and mass spectrometry information were carried out by analyst 1.6.2 software (AB SCIEX, USA). Chromatographic separation was achieved on a Waters ACQUITY UPLC BEH C18 column (2.1 mm × 100 mm inside diameter, 1.7 μm). The mobile phase system consisted of 0.1% formic acid in water (A) and acetonitrile (B) using a gradient elution as follows: 0 to 1.0 min, 10 to 90% B; held 90% B for 1 min. The flow rate was 0.5 ml/min, and the temperature of the column and autosampler was maintained at 35° and 15°C, respectively. The injection volume was 1 μl. In the MS analysis, positive ionization mode was used for sample detection, with the following optimized mass spectrometric parameters: ionspray voltage, 5500 V; declustering potential, 100 V; and temperature, 500°C. Eribulin, compound 1 , cevipabulin, and IS were conducted in multireaction monitoring mode with ion pairs of 730.4 > 680.4, 396.0 > 360.1, 465.0 > 358.2, and 265.2 > 232.2, respectively.
7
Targeted Proteomic Profiling of Coronary Heart Disease
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MRM-MS was performed in individual samples on an independent cohort (set 2, Table 1 ) consisting of 22 CHD and 20 control subjects. High-confidence peptides of the target proteins exhibiting rich product ion spectra were selected for MRMs. The analyses for all the experiments were performed on a QTRAP 5500 mass spectrometer instrument (AB SCIEX, Foster City, CA, USA) equipped with a Waters nano Acquity Ultra Performance LC system. We detected and verified transitions by MRM + Enhanced Product Ion (EPI) mode. ProteinPilot software (Applied Biosystems) was used to search protein database for MS/MS data generated from the MRM-MS assays. Twenty-four femtomoles of β-Galactosidase peptides were added to each of the 42 samples as internal standards46 (link)47 (link). Each of these samples were prepared in triplicate and processed in a randomized order. These replicate sample preparations were used to determine the CV of the MRM assay for each peptide. For detailed experimental procedures, see the online Supplemental material.
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