Peptides were synthesized by a standard solid-phase method using Syro I (Biotage, Uppsala, Sweden). Fmoc-protected amino acid-loaded resins and Fmoc-protected amino acids were purchased from Merck (Darmstadt, Germany). Additionally, 1-[Bis(dimethylamino)methylene]-1H-1,2,3-triazolo[4,5-b]pyridinium 3-oxide hexafluorophosphate (HATU, Merck) was used in the coupling reaction. After cleavage and deprotection of peptides using reagent K (trifluoroacetic acid/phenol/thioanisole/1,2-ethanedithiol, 82.5/5/5/2.5), cold diethyl ether was added to precipitate the peptides. Sequences were confirmed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) (TOF/TOF5800, AB SCIEX, Framingham, MA, USA).
Tof tof 5800
Manufactured by AB Sciex
Sourced in United States
The TOF/TOF 5800 is a high-performance mass spectrometry instrument designed for accurate and sensitive analysis of a wide range of samples. It features a tandem time-of-flight (TOF/TOF) configuration, allowing for precise mass measurements and effective fragmentation of analytes.
Automatically generated - may contain errors
Lab products found in correlation
Fmoc protected amino acid loaded resins, by Merck Group (2 mentions)
Syro 1, by Biotage (2 mentions)
Fmoc protected amino acids, by Merck Group (2 mentions)
Cm1950, by Leica (2 mentions)
Indium tin oxide coated glass slide, by Bruker (2 mentions)
Acquity uplc system, by Waters Corporation (1 mentions)
Drx 500 spectrometer, by Bruker (1 mentions)
Butylamine, by Merck Group (1 mentions)
Hexamethylenediamine, by Merck Group (1 mentions)
2 2 diphenyl 1 picrilhydrazyl dpph ferric chloride 3 hexahydrate, by Merck Group (1 mentions)
Sodium dithionite, by Merck Group (1 mentions)
Sphereclone ods, by Phenomenex (1 mentions)
V 730 spectrophotometer, by Jasco (1 mentions)
3 4 dihydroxy l phenylalanine l dopa, by Merck Group (1 mentions)
Potassium ferricyanide, by Merck Group (1 mentions)
Sodium bicarbonate, by Merck Group (1 mentions)
Avance 400 spectrometer, by Bruker (1 mentions)
Tec control chromatography strips, by Mirion Technologies (1 mentions)
17 protocols using tof tof 5800
1
Solid-Phase Peptide Synthesis and Characterization
2
Protein Identification by MALDI-TOF/TOF
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The selected protein spots were extracted, digested and analyzed by the MALDI-TOF/TOF analyzer (AB SCIEX TOF/TOF-5800, USA) as described previously (Wu et al., 2015 (link)). MALDI-TOF/TOF spectra were acquired in the positive ion mode and automatically submitted to Mascot 2.2 (http://www.matrixscience.com ) for identification against NCBInr database (version February 17, 2017; species, Zea mays, 279566 sequences). Only significant scores defined by Mascot probability analysis greater than “identity” were considered for assigning protein identity. All of the positive protein identification scores were significant (P < 0.05).
3
Mass Spectrometry Analysis of INH and LDC
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Matrix-assisted
lased desorption/ionization mass spectroscopy of pure INH and stearoyl–INH
LDC was obtained using an AB SCIEX TOF/TOF 5800. The experiment was
performed by dissolving pure INH in methanol and LDC in a mixture
of chloroform and methanol to determine the exact molecular weight
of the compounds by the soft ionization technique, as reported previously
in the literature.46 (link)
lased desorption/ionization mass spectroscopy of pure INH and stearoyl–INH
LDC was obtained using an AB SCIEX TOF/TOF 5800. The experiment was
performed by dissolving pure INH in methanol and LDC in a mixture
of chloroform and methanol to determine the exact molecular weight
of the compounds by the soft ionization technique, as reported previously
in the literature.46 (link)
4
Symbiodiniaceae Localization by MS Imaging
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Consecutive 10-μm sections were cut directly from the frozen samples using a cryostat (CM 1950; Leica Microsystems, Wetzlar, Germany). Serial sections were mounted onto glass slides for with/without hematoxylin and eosin (HE) staining and onto indium tin oxide-coated glass slides (Bruker Daltonics, Billerica, MA, USA) for MS imaging. The section without HE stain was observed under epifluorescent microscope (BX50, Olympus, Tokyo, Japan) to confirm the distribution/localization of Symbiodiniaceae cells in the section. After MS imaging, the sections were subjected to HE staining for morphological observation. Samples were prepared as previously described.46 (link),47 (link) Briefly, a matrix solution containing 50 mg/mL 2,5-dihydroxybenzoic acid in methanol: water (8:2, v/v) was used, with 1–2 mL prepared before use and sprayed uniformly over the frozen sections using an airbrush with a 0.2-mm nozzle (Procon Boy FWA Platinum; Mr. Hobby, Tokyo, Japan). MS analysis was performed using TOF/TOF 5800 (AB Sciex, Framingham, MA, USA) and SolariX Fourier-transform ion cyclotron resonance (FT-ICR) (Bruker Daltonics) mass spectrometers. To optimize FT-ICR MS, we set the mass range from m/z 400–1200 for DGCC/PC, and m/z 100-500 for GCC and the spatial resolution to 150 μm for mantle tissue and 220 μm for the frozen viscera of the animal.
5
Solid-Phase Peptide Synthesis Protocol
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Peptides were synthesized by standard solid-phase synthesis using a Syro I (Biotage, Uppsala, Sweden). Fmoc-protected amino acid-loaded resins and Fmoc-protected amino acids were purchased from Merck (Darmstadt, Germany). 1-[Bis(dimethylamino)methylene]-1H-1,2,3-triazolo[4,5-b]pyridinium 3-oxide hexafluorophosphate (HATU, Merck) was used in the coupling reaction. After cleavage and deprotection of peptides using reagent K (trifluoroacetic acid/phenol/thioanisole/1,2-ethanedithiol, 82.5/5/5/2.5), cold diethyl ether was added to precipitate the peptides. Sequences were confirmed by matrix-assisted laser desorption/ionization Time-of-flight mass spectrometry (MALDI-TOF MS) (TOF/TOF5800, AB SCIEX, Framingham, Massachusetts, USA).
6
Immunoconjugate Quality Control via HPLC
7
MALDI-TOF-MS Analysis of Reaction Products
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Matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF-MS) analysis was carried out on an AB SCIEX TOF/TOF 5800 instrument (AB SCIEX, Shanghai, China) using a neodymium: yttrium aluminum garnet (Nd: YAG) laser with the 355 nm wavelength in positive reflective modes. A 1 μL of the reaction liquid was pipetted onto a stainless-steel plate and dried under ambient conditions, then, a 0.5 μL of 2,5-dihydroxybenzoic acid (DHB) matrix suspension was dropped onto the layer of reaction liquid and further dried under ambient conditions. Liquid products were analyzed by MALDI-TOF-MS to detect the change of molecular weight after the reaction.
8
MALDI-TOF Mass Spectrometry of CarD Proteins
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Purified CarD (50 μM) or CarDHis or CarDtr were mixed with sinapinic acid matrix solution (50% Acetonitrile/50% water with 0.1% Trifluoroacetic acid) in 1:1 ratio and the mix was spotted on the MALDI plate. The spots were air dried and data were acquired in linear and positive ion mode keeping the laser intensity between 3000–3400 V (AB Sciex TOF/TOF 5800). The data were analyzed using Data Explorer software version 4.9 of Applied Biosystems.
9
MALDI-TOF Mass Spectrometry of Extract
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The MALDI-TOF mass spectrum of the extract was obtained as already reported [48 (link)]. Briefly, 100 μg of the sample was dissolved in 0.1 mL CHCl3/CH3OH, and 0.5 μL was loaded on the MALDI target together with 0.5 μL of a matrix solution of 2,5-dihydroxybenzoic acid (DHB). The positive ion spectrum was acquired in reflectron mode on an ABSCIEX TOF/TOF 5800 (AB SCIEX, Darmstadt, Germany) mass spectrometer equipped with an Nd:YLF laser.
10
Tissue Preparation for Mass Spectrometry Imaging
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Tissue sections (18 µm) were serially cut using a cryostat (CM1950, Leica Microsystems, Wetzlar, Germany). The sections were then mounted onto indium tin oxide coated glass slides (Bruker Daltonics, Germany) for MS imaging. The samples were prepared according to a previously published method [24 (link)] after being dipped into methanol to wash away any lipophilic molecules. Appropriate matrix solutions, including 50 mg/mL 2,5-dihydroxybenzoic acid in methanol/water (8:2, v/v), were used. The matrix solution (2.0 mL) was sprayed uniformly over the frozen sections using an airbrush with a 0.2 mm nozzle (Procon Boy FWA Platinum, Mr. Hobby, Tokyo, Japan). MS imaging analyses were performed using TOF/TOF 5800 (AB SCIEX, Framingham, MA, USA) in positive-ion mode for masses in the range of m/z 500‒2000. The ion images were constructed using the Datacube Explorer Software [25 (link)].
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