Low molecular weight peptides in samples withdrawn at the end of the in vitro gastrointestinal digestion were extracted by ultrafiltration with Amicon Ultra-4 nominal cut-off 3 kDa as previously described [28 (link)]. Nano LC/MS and tandem MS experiments were carried out on a 1200 Series Liquid Chromatographic two-dimensional system coupled with a 6520 Accurate-Mass Q-TOF LC/MS via a Chip Cube Interface (Agilent Technologies, Santa Clara, CA, USA). Chromatographic separation was performed on a ProtID-Chip-43 (II) including a 4 mm 40 nL enrichment column and a 43 mm × 75 μm analytical column, both packed with a Zorbax 300SB 5 μm C18 phase (Agilent Technologies, Santa Clara, CA, USA). The full description of the method is reported in Tagliazucchi et al. [15 (link)].
Protid chip 43 2
Manufactured by Agilent Technologies
Sourced in United States
The ProtID-Chip-43 (II) is a laboratory equipment designed for the identification and analysis of proteins. It utilizes advanced technology to enable efficient and accurate protein identification and characterization. The core function of the ProtID-Chip-43 (II) is to provide researchers with a reliable tool for protein analysis, without making claims about its intended use or performance.
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Lab products found in correlation
2 protocols using protid chip 43 2
1
Peptide Extraction and Analysis in Gastrointestinal Digestion
2
Quantification of Bioactive Tripeptides
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The identification and quantification of IPP and VPP were carried out on 2 µL of suitably diluted TCA-soluble supernatant through nanoLC-MS/MS experiments performed on a 1200 Series Liquid Chromatographic two-dimensional system coupled to a 6520 Accurate-Mass Q-TOF LC/MS (Agilent Technologies, Milano, Italy). Chromatographic separation was performed on a ProtID-Chip-43(II) including a 4 mm 40 nL enrichment column and a 43 mm x 75 mm analytical column, both packed with a C18 phase (Agilent Technologies). The mobile phase composition and the gradient were the same as reported by Solieri et al. (2015) . The mass spectrometer was tuned, calibrated and set with the same parameters as reported by Dei Più et al. (2014) . VPP and IPP were selectively fragmented using a mass to charge ratio of 312.18 and 326.21 (charge +1), respectively and identified by comparing the retention time and fragmentation spectra of a synthetic standard tripeptide. VPP and IPP was quantified according to Solieri et al. (2015) . The assignment process was complemented and validated by the manual inspection of MS/MS.
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