Evidence map›Paper›PMID 2117980›Full record

ArticleBritish journal of pharmacology1990

Cationic factors affecting phospholipase activities from human lung.

D A Yeats, Y S Bakhle

Open access · bronzeAbstract read
In one paragraph

Article in British journal of pharmacology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. 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

2 authors at 2 institutions in 1 country.

D A YeatsDepartment of Pharmacology, Hunterian Institute, Royal College of Surgeons, London.
Y S Bakhle
Royal College of Surgeons of England · GBThe Honourable Society of Lincoln's Inn · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

1. The effects of varying H+ and other cation concentrations on phospholipase activity were investigated on two particulate fractions from human lung, corresponding to the mitochondrial and microsomal fractions. 2. Three 14C-labelled substrates, arachidonyl-phosphatidylcholine (PC), -phosphatidylethanolamine (PE) and -phosphatidylinositol (PI) were used. 3. For two substrates, PE and PI, hydrolysis was maximal at pH 6, with either subcellular fraction. 4. Hydrolysis of all three substrates was strongly inhibited by EDTA and EGTA (10-25 mM). Addition of 2,2-dipyridyl, o-phenanthroline, 8-hydroxyquinoline or desferrioxamine (10 microM-1 mM) did not inhibit but often increased hydrolysis of all substrates. 5. Addition of Zn2+, as ZnCl2, (10 microM-1 mM) inhibited PE and PI, but not PC, hydrolysis. 6. The phospholipase activities from human lung appear to be dependent on Ca2+ for maximal activity and to be inhibited by other metal ions including Zn2+.

Indexed as

CalciumCationsChromatography, Ion ExchangeChromatography, Thin LayerEdetic AcidEgtazic AcidHumansHydrogen-Ion ConcentrationHydrolysisIn Vitro TechniquesLungPhosphatidylcholinesPhosphatidylethanolaminesPhosphatidylinositolsPhospholipasesSubcellular FractionsCalciumCationsEdetic AcidEgtazic AcidPhosphatidylcholinesPhosphatidylethanolaminesPhosphatidylinositolsPhospholipasesZinc

Identifiers

PMID2117980
PMCPMC1917788
OpenAlexW2144417950

What Socratic 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 Socratic graph.