Lcq electrospray ion trap mass spectrometer

Manufactured by Thermo Fisher Scientific

Sourced in United States

The LCQ electrospray ion-trap mass spectrometer is a laboratory instrument used for the analysis and identification of chemical compounds. It utilizes electrospray ionization to generate charged ions from the sample, which are then trapped and analyzed using a quadrupole ion trap mass analyzer. The core function of this equipment is to provide precise and sensitive mass spectrometric analysis of various types of samples.

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Lab products found in correlation

8453 diode array spectrophotometer, by Agilent Technologies (5 mentions) Jupiter c5, by Phenomenex (1 mentions) Prism 9, by GraphPad (1 mentions) Inova 500, by Agilent Technologies (1 mentions) Directdrive 600 mhz spectrometer, by Agilent Technologies (1 mentions) Mathematica, by Wolfram (1 mentions)

6 protocols using lcq electrospray ion trap mass spectrometer

Kinetic Assays and Spectroscopic Analyses

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Steady-state kinetic assays were performed on an Agilent 8453 diode-array spectrophotometer at 22 °C. Nonlinear regression data analysis was performed using the program Grafit (Erithacus Software Ltd., Staines, U.K.). Protein concentrations were determined by the Waddell method.^{22 (link)} Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was carried out on denaturing gels containing 12% polyacrylamide.^{23 (link)} The PCR was carried out on a Labnet MultiGene OptiMax Thermal Cycler (Labnet International, Inc., Edison, NJ). Electrospray ionization mass spectrometry was performed on an LCQ electrospray ion-trap mass spectrometer (Thermo, San Jose, CA), housed in the Institute for Cellular and Molecular Biology (ICMB) Protein and Metabolite Analysis Facility at the University of Texas. ¹H NMR spectroscopic experiments to examine possible dehalogenase activities were carried out as described elsewhere.^{24 (link)} Light scattering experiments were carried out as described.^{25 (link)}

Baas B.J., Medellin B.P., LeVieux J.A., de Ruijter M., Zhang Y.J., Brown S.D., Akiva E., Babbitt P.C, & Whitman C.P. (2019). Structural, Kinetic, and Mechanistic Analysis of an Asymmetric 4-Oxalocrotonate Tautomerase Trimer. Biochemistry, 58(22), 2617-2627.

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Peptide Mapping of Natural Skin Secretions

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A further five milligrams of lyophilised skin secretion were dissolved in 0.5 ml of 0.05% (v/v) trifluoroacetic acid (TFA)/water and clarified by centrifugation. The clear supernatant was subjected to reverse-phase HPLC on an analytical column (Jupiter C-5, 250 mm ×10 mm; Phenomenex, Cheshire, UK), eluted with a 0–80% linear gradient of acetonitrile containing 0.05% (v/v) TFA in 240 min at a flow rate of 1 ml/min. Absorbance was monitored at 214 nm. The peptide mapping of two natural occurring peptides was conducted using MS/MS fragmentation sequencing against the cDNA encoding peptide precursors by LCQ electrospray ion-trap mass spectrometer (Thermo Fisher Scientific, Waltham, MA, USA).

Zhu H., Ding X., Li W., Lu T., Ma C., Xi X., Wang L., Zhou M., Burden R, & Chen T. (2018). Discovery of two skin-derived dermaseptins and design of a TAT-fusion analogue with broad-spectrum antimicrobial activity and low cytotoxicity on healthy cells. PeerJ, 6, e5635.

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Mass Spectrometry and Kinetic Analysis of 4-OT

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Mass spectral data were obtained on an LCQ electrospray ion-trap mass spectrometer (Thermo, San Jose, CA) in the ICMB Protein and Metabolite core facility. The samples were prepared as described previously [21 (link)]. Kinetic data were obtained at 24 °C on an Agilent 8453 diode-array spectrophotometer. 4-OT was assayed using 3a, as previously reported [19 (link)–20 (link)]. Protein concentrations were determined by the Waddell method [22 (link)]. 4-OT was analyzed using tricine SDS-PAGE on 15% gels [23 (link)]. All other proteins were analyzed using TRIS-glycine SDS-PAGE on 12% gels [24 (link)]. Gels were run on a Bio-Rad Mini-Protean II gel electrophoresis apparatus.

Stack T.M., Jr. W.H, & Whitman C.P. (2017). Synthesis and enzymatic ketonization of the 5-(halo)-2-hydroxymuconates and 5-(halo)-2-hydroxy-2,4-pentadienoates. Beilstein Journal of Organic Chemistry, 13, 1022-1031.

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Molecular Techniques and Mass Spectrometry

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Techniques for standard molecular biology manipulations were based on methods described elsewhere.¹⁴ DNA sequencing was performed in the DNA Sequencing Facility in the Institute for Cellular and Molecular Biology (ICMB) at the University of Texas at Austin. Electrospray ionization mass spectrometry (ESI-MS) was carried out on an LCQ electrospray ion-trap mass spectrometer (Thermo, San Jose, CA) in the Proteomics Facility in the ICMB. Steady-state kinetic assays were performed on an Agilent 8453 diode-array spectrophotometer at 22 °C. Non-linear regression data analysis was performed using the program GraphPad Prism 9 (GraphPad Software. San Diego, CA). Protein concentrations were determined by the Waddell method.^{15 (link)} Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was carried out on denaturing gels containing 12% polyacrylamide.^{16 (link)} The sequence alignments and secondary information were visualized using ESPript version 3.0.^{17 (link)}

Jarvis E.D, & Nottebohm F. (1997). Motor-driven gene expression. Proceedings of the National Academy of Sciences of the United States of America, 94(8), 4097-4102.

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Steady-State Kinetic Assays and Protein Characterization

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Steady-state kinetic assays were performed on an Agilent 8453 diode-array spectrophotometer at 22 °C. Nonlinear regression data analysis was performed using the program Grafit (Erithacus Software Ltd., Staines, U.K.). Protein concentrations were determined by the Waddell method.^{24 (link)} SDS-PAGE was carried out on denaturing gels containing 12% polyacrylamide.^{25 (link)} Electrospray ionization mass spectrometry was performed on an LCQ electrospray ion-trap mass spectrometer (Thermo, San Jose, CA), housed in the ICMB Protein and Metabolite Analysis Facility at the University of Texas at Austin. Nuclear magnetic resonance (NMR) spectra were recorded on a Varian INOVA-500 or a Varian DirectDrive 600 MHz spectrometer (Palo Alto, CA). NMR signals were analyzed using the software program SpinWorks 3.1.6 (Copyright © 2009 Kirk Marat, University of Manitoba).

LeVieux J.A., Baas B.J., Kaoud T.S., Davidson R., Babbitt P.C., Zhang Y.J, & Whitman C.P. (2017). Kinetic and Structural Characterization of a cis-3-Chloroacrylic Acid Dehalogenase Homologue in Pseudomonas sp. UW4: A Potential Step Between Subgroups in the Tautomerase Superfamily. Archives of biochemistry and biophysics, 636, 50-56.

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Mass Spectrometry and Kinetic Analysis of 4-OT Enzyme

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Mass spectral data were obtained on an LCQ electrospray ion-trap mass spectrometer (Thermo, San Jose, CA) in the ICMB Protein and Metabolite core facility. The samples were prepared as described previously (19 (link)). Kinetic data were obtained at 24 °C on an Agilent 8453 diode-array spectrophotometer. 4-OT was assayed using 2-hydroxymuconate (2), as previously reported (18 (link)). Nonlinear regression data analysis was performed using Mathematica (Wolfram Research, Inc., Mathematica, Version 8.0, Champaign, IL 2010). Protein concentrations were determined by the Waddell method (20 (link)).

Stack T.M., Li W., Johnson WH J.r., Zhang Y.J, & Whitman C.P. (2018). Inactivation of 4-Oxalocrotonate Tautomerase by 5-Halo-2-hydroxy-2,4-pentadienoates. Biochemistry, 57(6), 1012-1021.

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