MS spectra were acquired using a matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometer (UltraFlex; Bruker Daltonik GmbH, Bremen, Germany). Ions were generated by a pulsed 337-nm nitrogen laser and accelerated to 20 kV. All spectra were obtained in the positive reflectron mode and analyzed using FlexAnalysis 2.0 software (Bruker Daltonik GmbH). Glycan signals were assigned using the GlycoMod tool (https://web.expasy.org/glycomod/ ). Tandem mass spectra were acquired using a MALDI-quadrupole ion trap (QIT)-TOF mass spectrometer (AXIMA-QIT; Shimadzu Corp., Kyoto, Japan) in the positive ion mode. Ions were generated using a 337-nm nitrogen laser and argon gas was used as the collision gas for collision-induced dissociation. For sample preparation, 0.5 μL of 2,5-dihydroxybenzoic acid (DHB, 044–29101; Fujifilm Wako Pure Chemical Corporation) solution (10 mg/mL in 30% ethanol) was spotted onto a MALDI target plate and dried. The permethylated glycans were dissolved in 50% acetonitrile, and 0.5-μL aliquots of the solution were spotted onto the dried DHB crystal on the target plate and air dried. Tandem mass spectra of the permethylated glycans were assigned using the GlycoWorkbench 2.1 suite of software tools (the European Carbohydrates Database [EUROCarbDB] project: http://www.eurocarbdb.org/ ).
Axima qit
Manufactured by Shimadzu
Sourced in Japan
The AXIMA-QIT is a mass spectrometer produced by Shimadzu. It utilizes a quadrupole ion trap (QIT) design for analytical applications. The AXIMA-QIT provides accurate mass measurement capabilities for a variety of sample types.
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Lab products found in correlation
6 protocols using axima qit
1
Glycan Structural Analysis by MALDI-TOF/QIT-TOF
2
MALDI-TOF and MALDI-QIT-TOF Mass Spectrometry of Glycans
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MS spectra were acquired using a matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometer (Ultraflex; Bruker Daltonik, Bremen, Germany). Ions were generated using a 337-nm nitrogen laser and were accelerated to 20 kV for reflectron mode and to 25 kV for linear mode. All spectra were obtained using a positive ion mode with delayed extraction. For MS/MS spectra acquisition, a MALDI-quadrupole ion trap (QIT)-TOF mass spectrometer (AXIMA-QIT; Shimadzu Corp., Kyoto, Japan) was used. Argon gas was used as a collision gas for collision-induced dissociation. For sample preparation, 0.5 μL of 2,5-dihydroxybenzoic acid (2,5-DHB; 10 mg/mL) in 30% ethanol was spotted onto a target plate (MTP 384 target plate ground steel [Bruker Daltonik] for Ultraflex and 384 specular surface stainless steel plate [Shimadzu Corp.] for AXIMA-QIT) and dried. For sialoglycans, at 95:5 mixture of 2,5-DHB and 2,5-DHB-Na was used as a matrix. Subsequently, an aliquot (0.5 μL) of the glycan solution was spotted onto the matrix crystal and dried.
3
Spatially-Resolved MALDI-MS Imaging of Metabolites
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Muscle tissues were sectioned at 10-μm thickness with a cryostat and thaw-mounted onto ITO-coated glass slides. 9-AA (600 mg) was deposited on slides at 0.5-μm thickness in an iMLayer (Shimadzu, Kyoto, Japan), and recrystallization was carried out by the methods described previously with slight modification47 (link). In this study, Matrix Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometer (MALDI-TOFMS, AXIMA® Confidence, Shimadzu) equipped with a 337 nm N2 laser was used for mass spectrometry analysis. Mass spectra were acquired with the laser frequency in the negative and scanning mass range from m/z 50 to m/z 1,000 at a high-resolution mode. Laser power, detection voltage, and accumulated number of MALDI-TOFMS were 115, 3.0 kV, and 1/pixel, respectively. The spatial interval of data points was 50 μm, giving 14641 profiles in total for the section. Data collected through the microscopic system were digitally processed using Imaging MS Solution analysis software (Shimadzu). The signal intensity of each imaging data in the figure is represented as the normalized intensity. Metabolites were identified with the MS/MS spectrum from results of IS chemical standard analysis using MALDI-QIT-TOFMS (AXIMA® QIT, Shimadzu).
4
Identifying Biomolecular Spectral Peaks
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To identify the spectral peaks, tandem mass spectrometry was performed using a MALDI-quadrupole ion trap—time of flight mass spectrometer (AXIMA-QIT; Shimadzu, Kyoto, Japan) [14 (link)]. The specific fragment patterns of phosphatidylcholine (PC), cholesterol ester, Heme B and ATP were identified according to previous reports [9 (link)] [15 (link)].
5
Radiation-Responsive Molecule Identification
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To identify candidate radiation-responsive molecules, we conducted MS/MS analysis, primarily with ultraflex TOF/TOF. Because of their ability to detect the peptide sequence, we further employed a MALDI-quadrupole ion trap (QIT)-TOF MS/MS (AXIMA-QIT; Shimadzu Scientific Instruments, Kyoto, Japan) or electrospray ionization (ESI)-Q-TOF MS (Q-STAR; Applied Biosystems, Foster City, CA, USA). After MS analysis, peptides were fragmented using the MS/MS mode. We performed MALDI-TOF MS using post-source decay by LIFT mode on the ultraflex. The MS/MS data we obtained were submitted to the Mascot Server to search against the mouse entries of the Mascot protein database (
http://www.matrixscience.com/ ).
For the identification of
m/z1721 (sodium adduct mass) and
m/z2821, we analyzed samples with the AXIMA-QIT using 2,5-dihydroxybenzoic acid as a matrix in the positive ion QIT collision-induced dissociation mode. We analyzed the results with the Shimadzu Biotech MALDI-MS software (Shimadzu Scientific Instruments).
Initially, we identified
m/z2821 using Q-STAR. We loaded each urine sample (5 µl) into a nano-spray tip (HUMANIX, Hiroshima, Japan). We used the reflector-positive mode to obtain all results. For protein identification, we used the obtained data to search against the mouse FASTA protein sequence database (
http://www.genome.jp/tools/fasta/ ).
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To identify candidate radiation-responsive molecules, we conducted MS/MS analysis, primarily with ultraflex TOF/TOF. Because of their ability to detect the peptide sequence, we further employed a MALDI-quadrupole ion trap (QIT)-TOF MS/MS (AXIMA-QIT; Shimadzu Scientific Instruments, Kyoto, Japan) or electrospray ionization (ESI)-Q-TOF MS (Q-STAR; Applied Biosystems, Foster City, CA, USA). After MS analysis, peptides were fragmented using the MS/MS mode. We performed MALDI-TOF MS using post-source decay by LIFT mode on the ultraflex. The MS/MS data we obtained were submitted to the Mascot Server to search against the mouse entries of the Mascot protein database (
For the identification of
m/z1721 (sodium adduct mass) and
m/z2821, we analyzed samples with the AXIMA-QIT using 2,5-dihydroxybenzoic acid as a matrix in the positive ion QIT collision-induced dissociation mode. We analyzed the results with the Shimadzu Biotech MALDI-MS software (Shimadzu Scientific Instruments).
Initially, we identified
m/z2821 using Q-STAR. We loaded each urine sample (5 µl) into a nano-spray tip (HUMANIX, Hiroshima, Japan). We used the reflector-positive mode to obtain all results. For protein identification, we used the obtained data to search against the mouse FASTA protein sequence database (
6
MALDI-TOF Analysis of Permethylated Glycans
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The MS spectra of the permethylated glycans were acquired in reflectron positive ion mode using a matrix-assisted laser desorption ionization (MALDI)-time-of-flight (TOF) mass spectrometer (UltraFlex; Bruker-Daltonics) equipped with a 337 nm pulsed nitrogen gas laser. 2,5-Dihydroxybenzoic acid (2,5-DHB) was used as the matrix. For sample preparation, 0.5 µl of 2,5-DHB solution (10 mg/ml in 30% ethanol) was deposited onto a MALDI target plate and dried. Then 0.5 µl of the sample solution was deposited over the dried spot of 2,5-DHB and dried. Tandem mass spectrometry was performed using a MALDI-quadrupole ion trap (QIT)-TOF mass spectrometer (AXIMA-QIT; Shimadzu Corp.) in a positive ion mode. Argon gas was used as the collision gas for collision-induced dissociation.
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