The LC-ESI-MS/MS system consisted of a Finnigan LTQ linear ion trap mass spectrometer (Thermo Fisher Scientific Inc.) coupled with an ESI interface, Paradigm MS4 pump (Michrom Bioresources Inc., Auburn, CA, USA) and an HTC PAL LC-autosampler (CTC Analytics GmbH, Zwingen, Switzerland). The parameters for analysis are shown below. The ion source voltage was set at 4.5 kV. The tube lens offset and capillary voltage were set at 90 V and 25 V, respectively. The capillary temperature was set at 275 °C. Nitrogen was used as sheath gas and auxiliary with 50 and 5 arbitrary units, respectively. Helium gas was used as the collision gas with a collisional activation amplitude of 35%. TSK gel ODS-100S (5 μm, 150 × 2.0 mm internal diameter, Tosoh Co., Tokyo, Japan) was used in reverse-phase mode. The mobile phase consisted of 0.1% formic acid (solvent A) and acetonitrile (solvent B) with linear gradient elution in 10–60% solvent B over 25 min at a flow rate of 200 μL/min. The injection volume was 10 µL.
Finnigan ltq linear ion trap mass spectrometer
Manufactured by Thermo Fisher Scientific
Sourced in United States
The Finnigan LTQ linear ion trap mass spectrometer is a laboratory instrument designed for the detection and analysis of chemical compounds. It utilizes linear ion trap technology to capture and analyze ions, providing high-sensitivity and high-resolution mass spectrometry capabilities.
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Lab products found in correlation
2 protocols using finnigan ltq linear ion trap mass spectrometer
1
LC-ESI-MS/MS Metabolite Analysis
2
Mass Spectrometry Analysis of Protein S-Nitrosylation
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The mass spectrometric analysis of protein S-nitrosylation residues was performed as described previously with minor modifications (Feng et al., 2013; Yang et al., 2015) . Briefly, purified His-PRMT5 protein labeled with Biotin-maleimide (Sigma, Cat#: B1267) was digested in-gel by trypsin (Promega, Cat#: V5280), and then analyzed by liquid chromatograph/mass spectrometry/mass spectrometry (LC-MS/MS) using a ThermoFisher Finnigan LTQ linear ion trap mass spectrometer. The raw data from mass spectrometry was searched against the NCBI Arabidopsis protein database using SEQUEST searching software. Cysteine biotinylation (451.200 Da), cysteine carbamidomethylation, and methionine oxidation were included in the search as the variable modifications.
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