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Cited by 49Advanced Proteomics Techniques and ApplicationsMass Spectrometry Techniques and ApplicationsMetabolomics and Mass Spectrometry Studies

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Evaluation of Interspecimen Trypsin Digestion Efficiency Prior to Multiple Reaction Monitoring-Based Absolute Protein Quantification with Native Protein Calibrators

van den Broek, Irene, Smit, Nico P. M., Romijn, Fred P. H. T. M., van der Laarse, Arnoud, Deelder, André M., van der Burgt, Yuri E. M., Cobbaert, Christa M.·2013·Journal of Proteome Research
DOI 10.1021/pr400763d
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Abstract

Implementation of quantitative clinical chemistry proteomics (qCCP) requires targeted proteomics approaches, usually involving bottom-up multiple reaction monitoring-mass spectrometry (MRM-MS) with stable-isotope labeled standard (SIS) peptides, to move toward more accurate measurements. Two aspects of qCCP that deserve special attention are (1) proper calibration and (2) the assurance of consistent digestion. Here, we describe the evaluation of tryptic digestion efficiency by monitoring various signature peptides, missed cleavages, and modifications during proteolysis of apolipoprotein A-I and B in normo- and hypertriglyceridemic specimens. Absolute quantification of apolipoprotein A-I and B was performed by LC-MRM-MS with SIS peptide internal standards at two time points (4 and 20 h), using three native protein calibrators. Comparison with an immunoturbidimetric assay revealed recoveries of 99.4 ± 6.5% for apolipoprotein A-I and 102.6 ± 7.2% for apolipoprotein B after 4 h of trypsin digestion. Protein recoveries after 20 h trypsin incubation equaled 95.9 ± 6.9% and 106.0 ± 10.0% for apolipoproteins A-I and B, respectively. In conclusion, the use of metrologically traceable, native protein calibrators looks promising for accurate quantification of apolipoprotein A-I and B. Selection of rapidly formed peptides, that is, with no or minor missed cleavages, and the use of short trypsin incubation times for these efficiently cleaved peptides are likely to further reduce the varia…

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Metadata

Authors
van den Broek, I., Smit, N. P. M., Romijn, F. P. H. T. M., van der Laarse, A., Deelder, A. M., van der Burgt, Y. E. M., & Cobbaert, C. M.
Affiliations
Leiden University Medical Center (NL)
Corresponding author
van den Broek, Irene
ORCID
Venue
Journal of Proteome Research
Publisher
American Chemical Society (ACS)
Published
2013-11-13
Volume
12
Issue
12
Pages
5760-5774
ISSN
  • 1535-3893 (ISSN-L)
  • 1535-3907
DOI
10.1021/pr400763d
OpenAlex
W2089526161
Cited by
49
References
0
Citations by year
2026: 1 · 2025: 1 · 2024: 5 · 2023: 2 · 2022: 4 · 2021: 3 · 2020: 6 · 2019: 4 · 2018: 2 · 2017: 4 · 2015: 12 · 2014: 4 · 2013: 1
FWCI
2.54
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Proteome Research (publishedVersion)
  • PubMed (publishedVersion)
  • Data Archiving and Networked Services (DANS) (submittedVersion)
  • Leiden Repository (Leiden University) (submittedVersion)
Topics
  • Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
  • Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolomics and Mass Spectrometry Studies
Keywords
apolipoprotein A-I, apolipoprotein B, absolute protein quantification, multiple reaction monitoring, isotope-labeled internal standards, missed cleavages, hypertriglyceridemia, traceability
MeSH terms
Amino Acid Sequence, Apolipoproteins B, Calibration, Chromatography, Liquid, Humans, Molecular Sequence Data, Nephelometry and Turbidimetry, Peptide Fragments, Reference Standards, Mass Spectrometry, Trypsin, Reproducibility of Results, Hypertriglyceridemia, Case-Control Studies, Apolipoprotein A-I, Proteolysis

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