Evidence map›Paper›PMID 31352127›Full record

ArticleRedox biology2019

Malondialdehyde interferes with the formation and detection of primary carbonyls in oxidized proteins.

Mario Estévez, Patricia Padilla, Leila Carvalho, Lourdes Martín, Ana Carrapiso, Josué Delgado

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
5.0field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 79 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Mario EstévezIPROCAR Research Institute, Faculty of Veterinary, University of Extremadura, 10003, Cáceres, Spain. Electronic address: mariovet@unex.es.
Patricia PadillaIPROCAR Research Institute, Faculty of Veterinary, University of Extremadura, 10003, Cáceres, Spain.
Leila CarvalhoPost-Graduate Program in Food Science and Technology, Federal University of Paraiba, João Pessoa, Brazil.
Lourdes MartínFood Technology, School of Agricultural Engineering, University of Extremadura, 06007, Badajoz, Spain.
Ana CarrapisoFood Technology, School of Agricultural Engineering, University of Extremadura, 06007, Badajoz, Spain.
Josué DelgadoIPROCAR Research Institute, Faculty of Veterinary, University of Extremadura, 10003, Cáceres, Spain; Heart Clinical Unit, Virgen de la Victoria University Clinic Hospital. Institute of Biomedical Research in Malaga. IBIMA. CIBERCV. University of Málaga, Málaga, Spain.
Universidad de Extremadura · ESUniversidad de Málaga · ESUniversidade Federal da Paraíba · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbonylation is one of the most remarkable expressions of the oxidative damage to proteins and the DNPH method the most common procedure to assess protein oxidation in biological samples. The present study was elicited by two hypotheses: i) is malondialdehyde, as a reactive dicarbonyl, able to induce the formation of allysine through a Maillard-type reaction? and ii) to which extent does the attachment of MDA to proteins interfere in the assessment of protein carbonyls using the DNPH method? Human serum albumin (HSA), human hemoglobin (HEM) and β-lactoglobulin (LAC) (5 mg/mL) were incubated with MDA (0.25 mM) for 24 h at 37 °C (HSA and HEM) or 80 °C (LAC). Results showed that MDA was unable to induce oxidative deamination of lysine residues and instead, formed stable and fluorescent adducts with proteins. Such adducts were tagged by the DNPH method, accounting for most of the protein hydrazones quantified. This interfering effect was observed in a wide range of MDA concentrations (0.05-1 mM). Being aware of its limitations, protein scientists should accurately interpret results from the DNPH method, and apply, when required, other methodologies such as chromatographic methods to detect specific primary oxidation products such as allysine.

Indexed as

2-Aminoadipic AcidHumansHydrazonesMalondialdehydeMetabolic Networks and PathwaysMolecular StructureOxidation-ReductionProtein CarbonylationProteins2-Aminoadipic AcidallysineHydrazonesMalondialdehydeProteinsAllysineCarbonylationDNPH methodMalondialdehydeProtein oxidation

Identifiers

PMID31352127
PMCPMC6669345
OpenAlexW2963484611

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.