For the chromatographic separation, 6530 Q-TOF LC/MS (Agilent Technologies) equipped with an autosampler (G7129A), a Quaternary Pump (G7104C), and a Column Compartment (G7116A) was used. The injection volume was 5 μL. The analytes were separated on a Zorbax RP-18 column (150 mm × 3 mm, 2.7 μm) in a flow rate of 0.3 mL/min. The mobile phase was composed of solvent A (aqueous formic acid, 0.1% v/v) and solvent B (0.1% formic acid/acetonitile). A gradient mode was implemented as follows; at t = 0–2 min, solvent A/solvent B (90/10); at t = 10 min, solvent A/solvent B, (80/20); at t = 52–80 min, 100% solvent B. Mass spectra were acquired using ESI in negative ionization mode with a capillary voltage of 4500 V. The mass spectra were recorded in the m/z range of 50–3000 m/z. The gas temperature and drying gas flow rate were 200 °C and 8 L/min, respectively. The skimmer and fragmentation voltages were set at 65 and 130 V, respectively, and collision energy was 10 V. The nebulization pressure was 58 psi. Data processing was performed using MassHunter workstation B.06.00 (Agilent Technologies, 2012) and compounds were tentatively identified according to their mass spectra, accurate mass and retention time, in comparison with literature.
6530 q tof lc ms
Manufactured by Agilent Technologies
Sourced in United States
The 6530 Q-TOF LC/MS is a high-resolution quadrupole time-of-flight mass spectrometer designed for liquid chromatography-mass spectrometry (LC-MS) applications. It provides accurate mass measurements and high-resolution separation of complex samples.
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Lab products found in correlation
6 protocols using 6530 q tof lc ms
1
Quantitative Metabolite Profiling by HPLC-MS
2
Recombinant Isotope-Labeled ZF5.3 Characterization
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13C & 15N-ZF5.3 was generated recombinantly as previously described, with the only difference being the use of U-13C glucose and 15NH4Cl (Cambridge Isotopes). For NMR experiments with 13C & 15N-ZF5.3, the protein was concentrated to 800 μM and buffer exchanged into Structure Determination Buffer . The homogeneity of 13C & 15N- ZF5.3 was analyzed via analytical size-exclusion chromatography. The molecular weight was examined on an Agilent 6530 QTOF LCMS.
3
LC-MS Analysis of Aqueous Extracts
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The chemical constituents of the aqueous extract were determined using LC-MS. LC-MS analysis was performed using 6530 Q-TOF LC/MS (Agilent Technologies) equipped with an autosampler (G7129A), a Quat. Pump (G7104C), and A Zorbax RP-18 column from Agilent Technologies (G7116A), 2.7 μ, (150 × 3 mm i.d.) was used for the analysis. Mobile phases were water (100%) as phase A and methanol (100%) as phase B, 0–2 min, isocratic 99% A, 2–16 min, linear gradient 99–94% A; 16–25 min, linear gradient 6–99% B; 25–30 min, isocratic 99% B. Solvents were delivered at a total flow rate of 0.4 ml/min. The MS spectra were acquired using ESI in both positive and negative ionization modes with a capillary voltage of 4000 V. The mass spectra were recorded in the m/z range of 100 to 2500 m/z. The gas temperature and drying gas flow were 320 OC and 10 L·/min, respectively. The skimmer and fragmentator voltages were set at 65 and 130 V, respectively and collision energy was 10 V. The nebulization pressure was 40 psig. A 4 μl volume of the extracts were injected onto the analytical column for analysis. The mass fragmentations were identified by using spectrum database for organic compounds in SDBS application.
4
Optimized LC-MS/MS Analysis of Compounds
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The LC-MS/MS experiments were carried out at the Faculty of Pharmacy, Fayoum University, using a 6530 Q-TOF LC/MS (Agilent Technologies, Santa Clara, CA, USA) outfitted with an autosampler (G7129A), a quat. pump (G7104C), and a column comp (G7116A). The extracts were separated on an Agilent Technologies Zorbax RP-18 column (150 mm 3 mm, dp = 2.7 m). The flow rate was 0.23 mL/min, and the injection volume was 2 L. The parameters were adjusted as previously described, and mass spectra were acquired using ESI in both ionization modes. A (water with 0.1% formic acid) and B (acetonitrile with 0.1% formic acid) served as the solvents. The following gradient elution times: 0–6 min; 5–50 min; 55–75 min; isocratic elution of 50% A: 50% B; and 75–140 min, were used for the linear gradient from 50% A: 50% B to 100% B.
5
Offline Extraction for HPLC-MS Analysis
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An offline extraction solution was prepared according to “Section 2.2 ” for HPLC-MS analysis. The chromatographic conditions were the same as that of the OMLE-HPLC system. HPLC-MS conditions: it was monitored by using an Agilent 6530 Q-TOF LC/MS (Palo Alto, CA, USA) equipped with an electrospray ionization (ESI) source operating in both positive and negative ions and an Agilent DAD detector (Santa Clara, CA, USA); dry gas (N2) flow of 8 L; dry gas temperature of 350°C; nebulizer of 38 psi; sheath gas flow rate of 11 min/L; capillary voltage of 3.5 kV; nozzle voltage of 1 kV. Collision energy was set at 10 V, 20 V, and 40 V, respectively.
6
Proteomic Analysis of Olea Europea
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The most bioactive OP-W extract was resuspended in 50 mM ammonium bicarbonate, pH 8.0, reduced with 10 mM DTT at 56 °C for 45 min, and alkylated with a 55 mM solution of iodoacetamide for 30 min at room temperature in the dark and then desalted by a SEP-PAK chromatography. The main fraction was manually collected and lyophilized. An aliquot of the sample was directly analyzed by LC-MS/MS for protein identification. The remaining portion of the lyophilized fraction was resuspended in 50 mM ammonium bicarbonate, pH 8.0, and incubated with trypsin in a 1/50 ratio (w/w) at 37 °C for 2 h. The sample was acidified with a final concentration of 0.2% trifluoracetic acid. The peptide mixture was first concentrated and desalted by C18 zip-tip and then was lyophilized. The lyophilized fraction was resuspended in 0.2% HCOOH and analyzed by LC-MS/MS, using a 6530 Q- TOF LC/MS (Agilent) system equipped with a nano-HPLC. After loading, peptide mixtures were first concentrated and desalted on the pre-column. For protein identification, the raw data obtained from the LC-MS/MS analysis were used to search both “Olea” and “Olea Europea” protein databases by an in-house version of the Mascot software.
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