All analyses of metabolites were performed by using a capillary electrophoresis time-of-flight mass spectrometry (CE-TOFMS) system (Agilent 7100 CE and 6210 TOFMS system, Agilent Technologies, Santa Clara, CA, USA) according to previous studies33 (link)34 (link)35 (link)36 (link). Metabolites were analyzed using a fused silica capillary (i.d. 50 μm × 80 cm), with commercial electrophoresis buffer as run and rinse buffer (product number H3301-1001 for cation analysis and I3302–1023 for anion analysis; Human Metabolome Technologies). The sample was injected at a pressure of 50 mbar for 10 sec for the cation analysis, and at 50 mbar for 25 sec for the anion analysis. The TOFMS detected mass-to-charge ratios (m/z) of 50–1000. In addition, analysis of clam metabolites was carried out by Human Metabolome Technology Inc. (Yamagata, Japan), and lipids in the samples were not removed because those did not affect CE-TOFMS analysis.
Agilent 7100 ce
Manufactured by Agilent Technologies
Sourced in United States, Germany
The Agilent 7100 CE is a capillary electrophoresis (CE) system designed for analytical separation and characterization of biomolecules, such as proteins, peptides, and nucleic acids. The instrument utilizes the principles of electrophoresis to separate analytes based on their size-to-charge ratio. The 7100 CE system provides high-resolution separation and accurate detection of various biomolecular species.
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Lab products found in correlation
4 protocols using agilent 7100 ce
1
Metabolomic Analysis of Clam Samples
2
Capillary Electrophoresis Analysis of Milk Proteins
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Protein separation was performed with a 7100 capillary electrophoresis (CE) system (Agilent Technologies Co., Santa Clara, CA, USA) using an unfused silica standard capillary, as described by [16 (link)]. In short, separations were performed after adding 0.017 M D,L-dithiothreitol (DTT) to the sample buffer on the day of sample preparation to disrupt disulfide bridges in the milk proteins. Milk (300 μL) was mixed with sample buffer (700 μL), incubated at room temperature for 1 h, and defatted by centrifugation for 10 min at 10,000× g (Himac CT 15R). UV-vis absorbance at a wavelength of 214 nm was used for detection. Calculation of the relative concentration of individual proteins was based on peak area and expressed as percentage of total integrated area in the electropherogram using Agilent 7100 CE, version Rev.C01.08(210) software.
3
Quantifying Monomer Precursors via CE
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The concentration of monomer precursors in the medium was measured using Agilent 7100 CE, a capillary electrophoresis (CE) system, equipped with a capillary tube (HPCE standard cap 50 μm id, 72 cm). The sample was injected for 4 s under a pressure of 50 mbar. The electrophoresis was performed at 25°C and -15 kV, with α-AFQ108 used as the running buffer (Otsuka Electronics Co., Ltd., Osaka, Japan). The sample was detected by a diode array at 400 nm.
4
Free-solution CE Analysis of RGDS Peptide
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Free-solution CE experiments were carried out using an Agilent 7100 CE (Agilent Technologies, Waldbronn, Germany) instrument equipped with a diode array detector.
Polyimide-coated fused silica high sensitivity capillaries (50 µm internal diameter) were purchased from Agilent. The electrolyte was sodium borate (75 mM, pH 9.2). The capillary (43.5 cm total length, 35 cm effective length) was pretreated by a 10 min flush with NaOH (1 M), and then 5 min successive flushes with NaOH (0.1 M), MilliQ water and sodium borate (75 mM, pH 9.2). The capillary surface was regenerated between separations through a 1 min flush with NaOH (1 M) then a 5 min flush with sodium borate (75 mM, pH 9.2). All injections were hydrodynamic, i.e., pressure (30 mbar) was applied for 10 s. Detection was set at 195 nm. Separation was obtained applying 30 kV at 25 °C. Each injected solution contained 0.22 vol% DMSO as an electroosmotic flow marker. An oligoacrylate with a known separation [36] and a broad range of mobilities was injected to validate the capillary and the instrument before each session.
The peptide consumption was calculated by determining the area under the curve of the identified RGDS peak divided by the migration time at each time interval and then normalizing it to the area determined for the aliquot just before the peptide mixture was introduced to the chitosan films.
Polyimide-coated fused silica high sensitivity capillaries (50 µm internal diameter) were purchased from Agilent. The electrolyte was sodium borate (75 mM, pH 9.2). The capillary (43.5 cm total length, 35 cm effective length) was pretreated by a 10 min flush with NaOH (1 M), and then 5 min successive flushes with NaOH (0.1 M), MilliQ water and sodium borate (75 mM, pH 9.2). The capillary surface was regenerated between separations through a 1 min flush with NaOH (1 M) then a 5 min flush with sodium borate (75 mM, pH 9.2). All injections were hydrodynamic, i.e., pressure (30 mbar) was applied for 10 s. Detection was set at 195 nm. Separation was obtained applying 30 kV at 25 °C. Each injected solution contained 0.22 vol% DMSO as an electroosmotic flow marker. An oligoacrylate with a known separation [36] and a broad range of mobilities was injected to validate the capillary and the instrument before each session.
The peptide consumption was calculated by determining the area under the curve of the identified RGDS peak divided by the migration time at each time interval and then normalizing it to the area determined for the aliquot just before the peptide mixture was introduced to the chitosan films.
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