Evidence map›Paper›PMID 7998991›Full record

ArticleThe Biochemical journal1994

Quantification of human serum paraoxonase by enzyme-linked immunoassay: population differences in protein concentrations.

M C Blatter Garin, C Abbott, S Messmer, M Mackness, P Durrington, D Pometta, R W James

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Biochemical journal, 1994. 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
4.4field-weighted citation impact, top 5% 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, 130 citations in OpenAlex.

  1. Article
  2. Review
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  11. Genetic polymorphisms in the Paraoxonase 1 gene and risk of ovarian epithelial carcinoma.Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology · 2008
    Article
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  18. Reconsideration of the catalytic center and mechanism of mammalian paraoxonase/arylesterase.Proceedings of the National Academy of Sciences of the United States of America · 1995
    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

7 authors at 1 institution in 1 country.

M C Blatter GarinDepartment of Medicine, University Hospital, Geneva, Switzerland.
C Abbott
S Messmer
M Mackness
P Durrington
D Pometta
R W James
University Hospital of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Paraoxonase is a serum protein bound to high-density lipoproteins (HDLs). The physiological function of the enzyme is unknown, but a role in lipid metabolism has been postulated. To date, studies of the protein have had to rely on measurements of enzyme activity with various substrates. We have developed a highly specific, competitive e.l.i.s.a. using a previously characterized monoclonal antibody. The assay can detect 20 ng of paraoxonase with a working range of 75-600 ng. Intra- and interassay coefficients of variation were 6.5 and 7.9% respectively. Serum concentrations of paraoxonase in healthy subjects from Geneva and Manchester ranged from 25 to 118 micrograms/ml. There were significant differences in mean concentrations between the two groups (Geneva, 79.3 +/- 18.7 micrograms/ml; Manchester, 59.9 +/- 24.1 micrograms/ml: P < 0.001), differences also apparent when subjects were compared according to paraoxonase phenotype. These appeared to be largely a consequence of differences in apolipoprotein A-I concentrations between the two populations, suggesting that HDL particle number may be important in determining serum levels of paraoxonase. Paraoxonase specific activities were also significantly different between the two groups of subjects (Geneva, 2.08 +/- 0.96 units/mg; Manchester, 3.08 +/- 1.73 units/mg: P < 0.001), which may reflect differences in HDL particle composition. The e.l.i.s.a. should furnish the necessary complement to studies of paraoxonase enzymic activity and has already provided evidence for differences with respect to serum levels of the protein both between populations and between phenotypes within populations.

Indexed as

AnimalsAntibodies, MonoclonalApolipoprotein A-IAryldialkylphosphataseEdetic AcidEgtazic AcidElectrophoresis, Gel, Two-DimensionalEnzyme-Linked Immunosorbent AssayEsterasesFemaleHumansImmunoblottingLipidsLipoproteins, HDLMaleMicrochemistryAntibodies, MonoclonalApolipoprotein A-IAryldialkylphosphataseEdetic AcidEgtazic AcidEsterasesLipidsLipoproteins, HDL

Identifiers

PMID7998991
PMCPMC1137527
OpenAlexW1800621346

What OpenQuestion holds

Textmetadata
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.