The polymerization degrees of BC-PANI and CC-PANI were analyzed using a MALDI-TOF/TOF MS 5800 System (AB SCIEX, USA) equipped with a 1 kHz Opti-BeamTM on-axis laser, and a MALDI-TOF Voyager DE-STR (Applied Biosystems, USA) system equipped with a 337-nm nitrogen laser in the linear positive mode, respectively. All samples were dissolved in a TA50 (50% acetonitrile/50% water with 0.1% TFA) solution and mixed with α-cyano-4-hydroxycinnamic acid (CHCA) or 2, 5-dihydroxybenzoic acid (DHB) as a matrix. The samples (0.5 μL) were placed in a 384 Opti-TOF stainless steel plate (AB SCIEX, USA).
Maldi tof voyager de str
Manufactured by Thermo Fisher Scientific
Sourced in United States
The MALDI-TOF Voyager DE-STR is a matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometer designed for high-throughput, high-resolution analysis of biomolecules. It utilizes a delayed extraction technique to improve mass resolution and accuracy.
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Lab products found in correlation
Maldi tof tof ms 5800 system, by AB Sciex (1 mentions)
Trypsin, by Promega (1 mentions)
Data explorer, by Thermo Fisher Scientific (1 mentions)
F 7000 fluorescence spectrophotometer, by Hitachi (1 mentions)
V 670, by Jasco (1 mentions)
Nicolet is50, by Thermo Fisher Scientific (1 mentions)
Ultrahydrogel 120 column, by Waters Corporation (1 mentions)
Trifluoroacetic acid, by Merck Group (1 mentions)
Sinapinic acid, by Merck Group (1 mentions)
Empower software, by Waters Corporation (1 mentions)
Alliance e2695 hplc, by Waters Corporation (1 mentions)
Hi9318, by Hanna Instruments (1 mentions)
Uv 3101pcuv vis nir scanning spectrophotometer, by Shimadzu (1 mentions)
Q exactive, by Thermo Fisher Scientific (1 mentions)
Spd 20a uv vis detector, by Shimadzu (1 mentions)
Wizard 2470, by PerkinElmer (1 mentions)
Crc 15r, by Mirion Technologies (1 mentions)
Flow count radiation detector, by Bioscan (1 mentions)
Lc 20at system, by Shimadzu (1 mentions)
9 protocols using maldi tof voyager de str
1
Polymerization Degrees Analysis of BC-PANI and CC-PANI
2
In-Gel Trypsin Digestion for Proteomic Analysis
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In-gel digestion was performed according to Applied Biosystems' instructions. The Coomassie blue-stained bands were cut out and washed with 50% acetonitrile/25 mM ammonium bicarbonate (pH 8.0) solution three times. Gels were dehydrated by soaking in 100% acetonitrile and dried in a vacuum centrifuge. The gel pieces were then incubated in 20 μL of digestion buffer containing 25 mM ammonium bicarbonate (pH 8.0) and 10 μg/mL of trypsin (Promega, Madison, WI, USA) in an ice-cold bath. After 30 minutes, the supernatant was removed and replaced with 10 μL of 25 mM ammonium bicarbonate buffer. Thereafter, the gel was incubated at 37℃ for 16 hours. Peptides were extracted twice with 30 μL of 50% acetonitrile/5% TFA solution for 60 minutes and dried in a vacuum centrifuge. Three microliters of the matrix (α-cyano–4 hydroxycinnamic acid) dissolved in 100% acetonitrile/0.1% TFA solution was mixed with the extracted peptides. Then, the peptide mixture (1 μL) was deposited on a MALDI plate and dried at room temperature. The peptide spectra were detected with MALDI-TOF Voyager DE-STR (Applied Biosystems, Framingham, CA, USA). The general procedure related to MALDI-TOF was carried out according to Applied Biosystems' instructions, and the peptide peaks were analyzed by searching the ProteinProspector MS-FIT database.
3
Phosphopeptide Identification and Validation
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Identification of phosphopeptides was performed as already described (55 (link)). Briefly, purified proteins were in gel-digested with trypsin, phosphopeptides enriched by IMAC following the manufacturer’s guidelines (Phosphopeptide Enrichment Kit; Pierce) and mass spectrometry analysis performed with a MALDI-TOF Voyager DE-STR (Applied Biosystems, Foster City, CA, USA) in positive reflectron mode, using phospho-DHB as matrix. MS spectra were processed with DATA EXPLORER (Applied Biosystems) and GPMAW software for peak to sequence assignments. To confirm the attribution of relative peaks to mono-, di- and tri-phosphorylated peptides, alkaline phosphatase treatment was performed on-probe as already described (56 (link)).
4
Characterization of Novel Organic Compounds
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All chemicals were purchased from commercial sources and used without further purification. 1H NMR spectra were recorded at 298 K on a 500 MHz JEOL JNM–ECZ 500R/S1 spectrometer. 1H NMR data are reported as follows: s: singlet, d: doublet, t: triplet, m: multiplet. Chemical shifts in the 1H NMR spectra are reported in parts per million (ppm) compared to a tetramethylsilane (0 ppm) standard. Matrix-assisted laser desorption ionization mass spectrometry (MALDI-TOF-MS) was conducted on a MALDI TOF Voyager DE-STR (Applied Biosystems, USA) mass spectrometer. Thin layer chromatography was performed using silica gel 60 F254 plates. Ultraviolet–visible (UV-vis) absorption spectra were measured with a UV-vis spectrophotometer (Jasco V-670). Fluorescence emission spectra were collected using a Hitachi F-7000 fluorescence spectrophotometer with excitation and emission slit widths of 5 nm. Column chromatography was performed using Merck silica gel (230–400 mesh).
5
Characterization of Lf-GL Conjugate
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Fourier transform infrared spectroscopy measurements (FT-IR, NICOLET IS50, Thermo Fisher Scientific) were conducted to identify the functional group of Lf-GL. The molecular weight of Lf-GL was determined by SDS-PAGE (12%-gel) and matrix-assisted laser desorption/ionization time-of-flight (MALDI TOF). MALDI-TOF was conducted at Seoul National University (Korea) using a MALDI-TOF Voyager DE-STR (Applied Biosystems, MA, USA). A sinapinic acid (Sigma-Aldrich) aqueous solution containing about 30% acetonitrile in 0.15% trifluoroacetic acid (Millipore) was used as a matrix. High performance liquid chromatography (Alliance HPLC e2695, Waters, MA, UK) using a gel permeation chromatography (GPC) column was performed to verify GL content in the Lf-GL conjugate. The mobile phase was composed of methanol, acetonitrile, water, and acetic acid in a ratio of 55:23.69:19.63:0.68. GL was dissolved in the mobile phase in different concentrations (2.5 to 200 × 10–6 M), and Lf-GL (25 × 10–6 M) was also dissolved in the mobile phase. Ultrahydrogel 120 Column (Waters) was used as a column, and the flow rate was 1 mL min−1. Then, absorbance was measured at 254 nm, and the results were calibrated with Empower software (Waters).
6
Zeta-Potential Characterization of Polyaniline
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For zeta-potential measurements, the pH of the polyaniline or aniline tetramer solution was tuned by adding NaOH. Values of pH were determined using a pH meter (HANNA, HI9318, Woonsocket, RI, USA). The DTS cell was placed in a Malvern Zetasizer (Nano ZS 3600, Worcestershire, UK) for measuring the zeta potential.
Mass spectra for devices were collected by carefully scraping materials off current collectors. The analyte was dissolved in a mixture of ethanol and dimethyl sulfoxide (1:1) solution. A matrix solution was prepared which contained 10 mg of 2,5-dihydroxybenzoic acid (DHB) dissolved in 50 μL of acetonitrile and 50 μL of 10% trifluoroacetic acid (TFA) in water. Equal volumes of each solution were pipetted, mixed and dried on the MALDI TOF plate. Spectra shown inFigure 3 were acquired with an Applied Biosystems Voyager-De-STR MALDI TOF. Subsequent spectra were acquired with a Bruker UltraFlex MALDI TOF (Bruker Daltonics Inc., Billerica, MA, US). The UV–vis spectra were taken on a Shimadzu UV-3101 PC UV–vis-NIR Scanning Spectrophotometer with quartz cuvettes. The Scanning electron microscope (SEM) images were taken on an FEI Nova 230 (FEI, Hillsboro, OR, USA).
Mass spectra for devices were collected by carefully scraping materials off current collectors. The analyte was dissolved in a mixture of ethanol and dimethyl sulfoxide (1:1) solution. A matrix solution was prepared which contained 10 mg of 2,5-dihydroxybenzoic acid (DHB) dissolved in 50 μL of acetonitrile and 50 μL of 10% trifluoroacetic acid (TFA) in water. Equal volumes of each solution were pipetted, mixed and dried on the MALDI TOF plate. Spectra shown in
7
Proteomic Analysis of Archaella Proteins
8
Radiolabeled Peptide Characterization
9
Analyzing ARDS BALF Peptides by MALDI-TOF/FTMS
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NBD-UBI or NBD-UBIdend were added to saline or pooled BALF from three patients with ARDS incubated for 30 min. ARDS BALF was retrieved from patients in ICU, as previously described34 (link). Samples were passed through ZipTip (C-18, 0.2 µL) conditioned with 5 µL MeCN (with 0.1% TFA as an additive) followed by 20 µL of H2O. The ZipTip was loaded with the sample, washed and eluted with 5 µL of 80% aq. MeCN (with 0.1% TFA as an additive). Samples were analysed on a MALDI-TOF (PerSeptive Biosystems Voyager DE™STR MALDI-TOF) mass spectrometer, Applied Biosystems, Foster City, CA) or FTMS (Bruker Daltonics 12 T SolariX Fourier Transform Ion Cyclotron Resonance Mass Spectrometer (FT-ICR MS)).
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