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Lc msd ion trap

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The LC/MSD ion trap is a liquid chromatography-mass spectrometry (LC/MS) system that uses an ion trap mass analyzer. It is designed for the identification and quantification of a wide range of compounds in complex samples. The core function of the LC/MSD ion trap is to separate, detect, and analyze chemical compounds based on their mass-to-charge ratio.

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1100 series LC/MSD ion trap mass spectrometer Agilent 1100 series LC/MSD XCT plus ion trap mass spectrometer LC-MSD trap VL ion-trap mass spectrometer Agilent 1100 series LC/MSD ion trap mass spectrometer Agilent 1100 Series LC/MSD high-performance ion trap mass spectrometer LC/MSD ion trap mass spectrometer

3 protocols using lc msd ion trap

1

HPLC Analysis of Biological Samples

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Samples were analyzed by reverse-phase HPLC. A liquid chromatographic system (HPLC; Agilent) with a solvent pump (Agilent 1100 binary pump) and UV-vis multiple wavelength detector (MWD-G1365B, was used. Chemstation®software was used for data acquisition, reporting, and analysis. The C-18 reverse phase column used for chromatographic separation was Zorbax (particle size 5 μ, pore size 10 nm, dimension 4.6 mm × 250 mm) of Agilent technologies. Mass spectral analysis of the perfusates, wherever required was done by Agilent LC-MSD ion trap in positive ion mode.
Yerasi N., Vurimindi H, & Devarakonda K. (2015). Frog intestinal perfusion to evaluate drug permeability: application to p-gp and cyp3a4 substrates. Frontiers in Pharmacology, 6, 141.
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2

Mass Spectrometric Analysis of Peptides

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The peptides were analyzed on a LC/MSD ion trap (Agilent). ESI-MS spectra were acquired in positive ion mode. The solvent contained 40 % acetonitrile and 0.1 % formic acid. 10 to 30 µL sample were directly injected at a flow rate of 10 µL/min with a source temperature of 300 °C. The applied spray voltage was 3500 V, and the skimmer voltage 40 V. MS scans were acquired over an m/z range of 200 to 2000. The scan for the native mass 1499.69 Da of the sequence Tyr-Gly-Gly-Ser-Ala-Ala-Glu-Ala-Phe-Ala-Lys-Ala-Met-Ala-Arg, shows the single charged ion with m/z 1500.0 and the double charged ion m/z 750.7. The scan for the Met(O)-Phe sequence pair (1515.69 Da) shows the singly charged ion with m/z 1515.7, the double charged ion m/z 758.4, and the triple charged ion m/z 505.9. The observed masses for the respective molecular ions agree with the theoretical peptide scaffold design.
Lewis A.K., Dunleavy K., Senkow T.L., Her C., Horn B.T., Jersett M.A., Mahling R., McCarthy M.R., Perell G.T., Valley C.C., Karim C.B., Gao J., Pomerantz W.C., Thomas D.D., Cembran A., Hinderliter A, & Sachs J.N. (2016). Oxidation increases the strength of the methionine-aromatic interaction. Nature chemical biology, 12(10), 860-866.
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3

Mass Spectrometric Analysis of Peptides

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The peptides were analyzed on a LC/MSD ion trap (Agilent). ESI-MS spectra were acquired in positive ion mode. The solvent contained 40 % acetonitrile and 0.1 % formic acid. 10 to 30 µL sample were directly injected at a flow rate of 10 µL/min with a source temperature of 300 °C. The applied spray voltage was 3500 V, and the skimmer voltage 40 V. MS scans were acquired over an m/z range of 200 to 2000. The scan for the native mass 1499.69 Da of the sequence Tyr-Gly-Gly-Ser-Ala-Ala-Glu-Ala-Phe-Ala-Lys-Ala-Met-Ala-Arg, shows the single charged ion with m/z 1500.0 and the double charged ion m/z 750.7. The scan for the Met(O)-Phe sequence pair (1515.69 Da) shows the singly charged ion with m/z 1515.7, the double charged ion m/z 758.4, and the triple charged ion m/z 505.9. The observed masses for the respective molecular ions agree with the theoretical peptide scaffold design.
Lewis A.K., Dunleavy K., Senkow T.L., Her C., Horn B.T., Jersett M.A., Mahling R., McCarthy M.R., Perell G.T., Valley C.C., Karim C.B., Gao J., Pomerantz W.C., Thomas D.D., Cembran A., Hinderliter A, & Sachs J.N. (2016). Oxidation increases the strength of the methionine-aromatic interaction. Nature chemical biology, 12(10), 860-866.
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