Evidence map›Paper›PMID 24006961›Full record

ArticleMolecular pharmaceutics2013

Absolute quantification of aldehyde oxidase protein in human liver using liquid chromatography-tandem mass spectrometry.

John T Barr, Jeffrey P Jones, Carolyn A Joswig-Jones, Dan A Rock

Abstract read
In one paragraph

Article in Molecular pharmaceutics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

11 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. Aldehyde Oxidase Contributes to All-Drug metabolism and disposition: the biological fate of chemicals · 2021
    Article
  4. Article
  5. Time Course of Aldehyde Oxidase and Why It Is Nonlinear.Drug metabolism and disposition: the biological fate of chemicals · 2019
    Article
  6. Review
  7. Structure-metabolism relationships inProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  8. Molybdenum-containing nitrite reductases: Spectroscopic characterization and redox mechanism.Redox report : communications in free radical research · 2017
    Review
  9. Article
  10. Article
  11. Why do most human liver cytosol preparations lack xanthine oxidase activity?Drug metabolism and disposition: the biological fate of chemicals · 2014
    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 at 2 institutions in 1 country.

John T BarrDepartment of Chemistry, Washington State University , P.O. Box 644630, Pullman, Washington 99164-4630, United States.
Jeffrey P Jones
Carolyn A Joswig-Jones
Dan A Rock
Washington State University · USAmgen (United States) · US

Funding

Understanding the Metabolic Impact of Aldehyde Oxidase on New Drug DesignR01GM100874 · NIGMS · WASHINGTON STATE UNIVERSITY · PI JONES, JEFFREY P · 2012 to 2019
$2.6M
NIGMS NIH HHS GM100874NIGMS NIH HHS R01 GM100874
6 · The paper itself

Abstract

The function of the enzyme human aldehyde oxidase (AOX1) is uncertain; however, recent studies have implicated significant biochemical involvement in humans. AOX1 has also rapidly become an important drug-metabolizing enzyme. Until now, quantitation of AOX1 in complex matrices such as tissue has not been achieved. Herein, we developed and employed a trypsin digest and subsequent liquid chromatography-tandem mass spectrometry analysis to determine absolute amounts of AOX1 in human liver. E. coli expressed human purified AOX1 was used to validate the linearity, sensitivity, and selectivity of the method. Overall, the method is highly efficient and sensitive for determination of AOX1 in cytosolic liver fractions. Using this method, we observed substantial batch-to-batch variation in AOX1 content (21-40 pmol AOX1/mg total protein) between various pooled human liver cytosol preparations. We also observed interbatch variation in Vmax (3.3-4.9 nmol min(-1) mg(-1)) and a modest correlation between enzyme concentration and activity. In addition, we measured a large difference in kcat/Km, between purified (kcat/Km of 1.4) and human liver cytosol (kcat/Km of 15-20) indicating cytosol to be 11-14 times more efficient in the turnover of DACA than the E. coli expressed purified enzyme. Finally, we discussed the future impact of this method for the development of drug metabolism models and understanding the biochemical role of this enzyme.

Indexed as

Aldehyde OxidaseChromatography, High Pressure LiquidChromatography, LiquidHumansKineticsLiverMolecular StructureTandem Mass SpectrometryAldehyde Oxidase

Identifiers

PMID24006961
PMCPMC3883672
OpenAlexW2027522198

What OpenQuestion holds

Textmetadata
LicenceTDM
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.