Evidence map›Paper›PMID 31110556›Full record

ArticlePlant methods2019

Accurate and efficient amino acid analysis for protein quantification using hydrophilic interaction chromatography coupled tandem mass spectrometry.

Shrikaar Kambhampati, Jia Li, Bradley S Evans, Doug K Allen

Abstract read
In one paragraph

Article in Plant methods, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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

38 citing papers in PubMed.

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  17. Frontiers in nutrition · 2024
    Review
  18. Article
  19. Fortification ofBiotechnology reports (Amsterdam, Netherlands) · 2023
    Article
  20. Article
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

4 authors.

Shrikaar Kambhampati1Donald Danforth Plant Science Center, St. Louis, MO USA.
Jia Li1Donald Danforth Plant Science Center, St. Louis, MO USA.
Bradley S Evans1Donald Danforth Plant Science Center, St. Louis, MO USA.
Doug K Allen1Donald Danforth Plant Science Center, St. Louis, MO USA.ORCID 0000-0001-8599-8946

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMethods used to quantify protein from biological samples are often inaccurate with significant variability that requires care to minimize. The errors result from losses during protein preparation and purification and false detection of interfering compounds or elements. Amino acid analysis (AAA) involves a series of chromatographic techniques that can be used to measure protein levels, avoiding some difficulties and providing specific compositional information. However, unstable derivatives, that are toxic and can be costly, incomplete reactions, inadequate chromatographic separations, and the lack of a single hydrolysis method with sufficient recovery of all amino acids hinder precise protein quantitation using AAA.

resultsIn this study, a hydrophilic interaction chromatography based method was used to separate all proteinogenic amino acids, including isobaric compounds leucine and isoleucine, prior to detection by multiple reaction monitoring with LC-MS/MS. Through inclusion of commercially available isotopically labeled (

conclusionsAccurate determination of protein quantity and amino acid composition in heterogeneous biological samples is non-trivial. Recent advances in chromatographic phases and LC-MS/MS based methods, along with the availability of isotopic standards can minimize difficulties in analysis and improve protein quantitation. A robust method is described for high-throughput protein quantification and amino acid compositional analysis. Since accurate measurement of protein quality and quantity are a requirement for many biological studies that relate to crop improvement or more generally, our understanding of metabolism in living systems, we envision this method will have broad applicability.

Indexed as

Amino acidsChromatographyHILICIsobaric compoundsIsotopesLC–MS/MSProtein hydrolysisProtein quantificationSoybeans

Identifiers

PMID31110556
PMCPMC6511150

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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.