Evidence map›Paper›PMID 6321330›Full record

ArticleImmunology1984

Myeloperoxidase is more efficient than eosinophil peroxidase in the in vitro killing of newborn larvae of Trichinella spiralis.

J Buys, R Wever, E J Ruitenberg

Open access · greenAbstract read
In one paragraph

Article in Immunology, 1984. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

10 citing papers in PubMed, 41 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

3 authors.

J Buys
R Wever
E J Ruitenberg

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myeloperoxidase (MPO) and eosinophil peroxidase (EPO) catalyse the formation of hypochlorite (OCl-) from chloride ions (OCl-) and hydrogen peroxide (H2O2). OCl- proved to be highly toxic for Trichinella spiralis newborn larvae (NBL) in in vitro assays. Using purified human MPO and EPO it was found that even at neutral pH both enzymes under appropriate conditions are able to kill NBL. The rate at which OCl- is produced is much lower in the EPO- than in the MPO-mediated reaction. This difference in enzymic activity may explain why in the MPO-mediated reaction half the amount of OCl- was sufficient to kill 50% of the NBL, as compared to the EPO-mediated reaction. Purified human eosinophil major basic protein showed excellent OCl- scavenging properties, resulting in a significant decrease in the EPO-mediated NBL killing. Addition of ammonium ions [(NH4)2SO4] to the EPO-mediated reaction increased the NBL killing remarkably. It was concluded that in vitro MPO is more efficient than EPO in killing NBL. Furthermore, it was suggested that although eosinophils show marked parasiticidal effects in various in vitro systems, their primary biological role might be the regulation of the inflammatory reactions.

Indexed as

Antinematodal AgentsAnimalsEosinophil PeroxidaseHypochlorous AcidLarvaPeroxidasePeroxidasesQuaternary Ammonium CompoundsTrichinellaAntinematodal AgentsEosinophil PeroxidaseHypochlorous AcidPeroxidasePeroxidasesQuaternary Ammonium Compounds

Identifiers

PMID6321330
PMCPMC1454451
OpenAlexW2247661657

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.