Evidence map›Paper›PMID 35320366›Full record

ArticleAnalytical and bioanalytical chemistry2022

Determination of the protein content of complex samples by aromatic amino acid analysis, liquid chromatography-UV absorbance, and colorimetry.

Kathrin Reinmuth-Selzle, Teodor Tchipilov, Anna T Backes, Georg Tscheuschner, Kai Tang, Kira Ziegler, Kurt Lucas, Ulrich Pöschl, Janine Fröhlich-Nowoisky, Michael G Weller

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Article in Analytical and bioanalytical chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.9field-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

32 citing papers in PubMed, 74 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

10 authors at 2 institutions in 1 country.

Kathrin Reinmuth-SelzleMultiphase Chemistry Department, Max Planck Institute for Chemistry, 55128, Mainz, Germany.ORCID http://orcid.org/0000-0001-7274-3848
Teodor TchipilovDivision 1.5 Protein Analysis, Federal Institute for Materials Research and Testing (BAM), 12489, Berlin, Germany.ORCID http://orcid.org/0000-0003-0755-8595
Anna T BackesMultiphase Chemistry Department, Max Planck Institute for Chemistry, 55128, Mainz, Germany.ORCID http://orcid.org/0000-0002-2163-8973
Georg TscheuschnerDivision 1.5 Protein Analysis, Federal Institute for Materials Research and Testing (BAM), 12489, Berlin, Germany.ORCID http://orcid.org/0000-0002-2311-1016
Kai TangMultiphase Chemistry Department, Max Planck Institute for Chemistry, 55128, Mainz, Germany.ORCID http://orcid.org/0000-0002-5402-0344
Kira ZieglerMultiphase Chemistry Department, Max Planck Institute for Chemistry, 55128, Mainz, Germany.ORCID http://orcid.org/0000-0003-1368-9487
Kurt LucasMultiphase Chemistry Department, Max Planck Institute for Chemistry, 55128, Mainz, Germany.ORCID http://orcid.org/0000-0001-8267-7397
Ulrich PöschlMultiphase Chemistry Department, Max Planck Institute for Chemistry, 55128, Mainz, Germany.ORCID http://orcid.org/0000-0003-1412-3557
Janine Fröhlich-NowoiskyMultiphase Chemistry Department, Max Planck Institute for Chemistry, 55128, Mainz, Germany.ORCID http://orcid.org/0000-0002-1278-0054
Michael G WellerDivision 1.5 Protein Analysis, Federal Institute for Materials Research and Testing (BAM), 12489, Berlin, Germany. michael.weller@bam.de.ORCID http://orcid.org/0000-0003-2767-2029
Max Planck Institute for Chemistry · DEFederal Institute For Materials Research and Testing · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fast and accurate determination of the protein content of a sample is an important and non-trivial task of many biochemical, biomedical, food chemical, pharmaceutical, and environmental research activities. Different methods of total protein determination are used for a wide range of proteins with highly variable properties in complex matrices. These methods usually work reasonably well for proteins under controlled conditions, but the results for non-standard and complex samples are often questionable. Here, we compare new and well-established methods, including traditional amino acid analysis (AAA), aromatic amino acid analysis (AAAA) based on the amino acids phenylalanine and tyrosine, reversed-phase liquid chromatography of intact proteins with UV absorbance measurements at 220 and 280 nm (LC-220, LC-280), and colorimetric assays like Coomassie Blue G-250 dye-binding assay (Bradford) and bicinchoninic acid (BCA) assay. We investigated different samples, including proteins with challenging properties, chemical modifications, mixtures, and complex matrices like air particulate matter and pollen extracts. All methods yielded accurate and precise results for the protein and matrix used for calibration. AAA, AAAA with fluorescence detection, and the LC-220 method yielded robust results even under more challenging conditions (variable analytes and matrices). These methods turned out to be well-suited for reliable determination of the protein content in a wide range of samples, such as air particulate matter and pollen.

Indexed as

ColorimetryProteinsAmino AcidsAmino Acids, AromaticChromatography, LiquidParticulate MatterAmino AcidsAmino Acids, AromaticParticulate MatterProteinsAir particulate matterAromatic amino acid analysisAtmospheric aerosolChemical protein modificationLC-UV absorbancePollen extractProtein quantification

Identifiers

PMID35320366
PMCPMC9142416
OpenAlexW4220968438

What OpenQuestion holds

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LicenceCC BY
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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.