The efficiency of ZnPc-BSA conjugation was studied using a time-of-flight mass spectrometer with matrix laser desorption/ionization (MALDI-TOF/TOF) rapifleX MALDITOF/TOF MS System (Bruker Daltonik GmbH, Bremen, Germany). The operating mode was the following: linear mode, positive ionization, analysis range m/z 5000–70,000, accelerating voltage 20 kV, SmartBeam III laser, laser frequency 10 kHz, frequency 200 Hz. Before analysis, the device was calibrated using a mixture of proteins “Protein Calibration Standard I” (Bruker Daltonik GmbH, Germany). The mixture included the following proteins: insulin ([M+H] = m/z 5734.5), ubiquitin I ([M + H] = m/z 8565.76), cytochrome C ([M+H] = m/z 12,361.2), myoglobin ([M+H] = m/z 16,952.5). 2.5-dihydroxybenzoic acid (Bruker Daltonik GmbH, Germany) with purity > 99.0% was used as the matrix. A 20 mg/mL matrix solution was prepared in a mixture of 30% acetonitrile: 70% water: 0.1% trifluoroacetic acid. Aqueous solutions of the samples were mixed with the matrix in a ratio of 1:1, and 1 μL of the mixture was applied to the plate.
Rapiflex malditof tof ms system
Manufactured by Bruker
Sourced in Germany
The RapifleX MALDI-TOF/TOF MS System is a high-performance mass spectrometry platform designed for applications in proteomics, metabolomics, and other analytical fields. It provides accurate mass determination and fragmentation analysis of a wide range of molecules, enabling comprehensive structural characterization and identification.
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2 protocols using rapiflex malditof tof ms system
1
Characterization of ZnPc-BSA Conjugation
2
MALDI-TOF/TOF MS Proteomic Analysis
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The analysis was performed
using a rapifleX MALDI-TOF/TOF MS system (Bruker Daltonik GmbH, Germany)
time-of-flight mass spectrometer with matrix laser desorption/ionization
(MALDI-TOF/TOF). The operating mode was the following: reflector mode,
positive ionization, analysis range m/z 400–3000, accelerating voltage 20 kV, SmartBeam III laser,
laser frequency 10 kHz, and frequency 200 Hz. Before analysis, the
instrument was calibrated using a mixture of peptides “Peptide
Calibration Standard II” (Bruker Daltonik GmbH, Germany). The
mixture included peptides with a mass range of 700–3200 Da.
2,5-Dihydroxybenzoic acid (Bruker Daltonik GmbH, Germany) with purity
>99.0% was used as a matrix. A matrix solution with a concentration
of 20 mg/mL was prepared in a mixture of 30% acetonitrile/70% water/0.1%
trifluoroacetic acid. Aqueous solutions of the samples were mixed
with the matrix in a ratio of 1:1, and 1 μL of the mixture was
applied to the plate.
using a rapifleX MALDI-TOF/TOF MS system (Bruker Daltonik GmbH, Germany)
time-of-flight mass spectrometer with matrix laser desorption/ionization
(MALDI-TOF/TOF). The operating mode was the following: reflector mode,
positive ionization, analysis range m/z 400–3000, accelerating voltage 20 kV, SmartBeam III laser,
laser frequency 10 kHz, and frequency 200 Hz. Before analysis, the
instrument was calibrated using a mixture of peptides “Peptide
Calibration Standard II” (Bruker Daltonik GmbH, Germany). The
mixture included peptides with a mass range of 700–3200 Da.
2,5-Dihydroxybenzoic acid (Bruker Daltonik GmbH, Germany) with purity
>99.0% was used as a matrix. A matrix solution with a concentration
of 20 mg/mL was prepared in a mixture of 30% acetonitrile/70% water/0.1%
trifluoroacetic acid. Aqueous solutions of the samples were mixed
with the matrix in a ratio of 1:1, and 1 μL of the mixture was
applied to the plate.
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