Analysis of protein carbonylation — pitfalls and promise in commonly used methods
Open accessAbstract
Oxidation of proteins has received a lot of attention in the last decades due to the fact that they have been shown to accumulate and to be implicated in the progression and the pathophysiology of several diseases such as Alzheimer, coronary heart diseases, etc. This has also resulted in the fact that research scientists are becoming more eager to be able to measure accurately the level of oxidized protein in biological materials, and to determine the precise site of the oxidative attack on the protein, in order to get insights into the molecular mechanisms involved in the progression of diseases. Several methods for measuring protein carbonylation have been implemented in different laboratories around the world. However, to date no methods prevail as the most accurate, reliable, and robust. The present paper aims at giving an overview of the common methods used to determine protein carbonylation in biological material as well as to highlight the limitations and the potential. The ultimate goal is to give quick tips for a rapid decision making when a method has to be selected and taking into consideration the advantage and drawback of the methods.
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Protein carbonyls, 3-nitrotyrosine and methionine sulfoxide are biomarkers of protein oxidation commonly analyzed via immunochemical methods.
“Protein carbonyls, 3-NT and methionine sulfoxide are biomarkers of protein oxidation which are commonly analyzed via immunochemical methods [75,82,92].”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [75]
The indexed title identifies the paper as an analysis of protein carbonylation methods, and its keywords include “immunoaffinity.” The available passages do not say that immunochemical methods are commonly used for protein carbonyls, or address 3-nitrotyrosine or methionine sulfoxide; the broader claim is therefore not established by this copy. (LLM, conf=0.72)
Experimental — accuracy not yet measuredUnbound DNPH absorbs at the same wavelength as hydrazones (λ = 370 nm), requiring washing steps that cause an inevitable loss of protein of up to 10-15%.
“Unbound DNPH needs to be removed from the sample, because it absorbs at the same wavelength as hydrazones (λ = 370 nm). Several washing steps of the protein are required to remove unbound DNPH leading to an inevitable loss of protein of up to 10–15% [75].”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [75]
The indexed passages are bibliographic records and keywords, with no substantive passage on DNPH absorbance or washing-related protein loss. Searches for DNPH, 370 nm, and 10–15% protein loss found no passage that verifies the claim. (LLM, conf=0.72)
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Cites
Selected reaction monitoring–based proteomics: workflows, potential, pitfalls and future directions
Picotti, P., & Aebersold, R. (2012) · Nature Methods · doi:10.1038/nmeth.2015 · Cited by 1,302 · see citing works
Decoding protein modifications using top-down mass spectrometry
Siuti, N., & Kelleher, N. L. (2007) · Nature Methods · doi:10.1038/nmeth1097 · Cited by 503 · see citing works
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Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases
Kehm, R., Baldensperger, T., Raupbach, J., & Höhn, A. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101901 · Cited by 348 · see citing works
“9 of the protein are required to remove unbound DNPH leading to an inevitable loss of protein of up to 10–15% [75].”
BackgroundMethodInfluential
- Authors
- Rogowska-Wrzesinska, A., Wojdyla, K., Nedić, O., Baron, C. P., & Griffiths, H. R.
- Affiliations
- University of Belgrade (RS)
- Technical University of Denmark (DK)
- Aston University (GB)
- Venue
- Free Radical Research
- Publisher
- Informa UK Limited
- Published
- 2014-08-11
- Volume
- 48
- Issue
- 10
- Pages
- 1145-1162
- ISSN
- 1029-2470 (ISSN-L)
- 1071-5762
- OpenAlex
- W2167302232
- Cited by
- 65
- References
- 2
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 6 · 2023: 2 · 2022: 3 · 2021: 7 · 2020: 6 · 2019: 9 · 2018: 5 · 2017: 4 · 2016: 7 · 2015: 8 · 2014: 1
- FWCI
- 0.63
- Type
- journal article
- Language
- en
- Open access
- green
- orbit.dtu.dk
- Licence
- other-oa
- Locations
- Free Radical Research (publishedVersion)
- PubMed (publishedVersion)
- Aston Publications Explorer (Aston University) (acceptedVersion)
- Technical University of Denmark, DTU Orbit (Technical University of Denmark, DTU) (submittedVersion, other-oa)
- University of Southern Denmark Research Portal (University of Southern Denmark) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Keywords
- protein carbonylation, protein oxidation, method comparison, method selection, methodological limitations, biological specimen, disease progression
- MeSH terms
- Proteomics, Protein Carbonylation
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