Evidence map›Paper›PMID 9182718›Full record

ArticleThe Biochemical journal1997

Purification of a dichlorophenol-indophenol oxidoreductase from rat and bovine synaptic membranes: tight complex association of a glyceraldehyde-3-phosphate dehydrogenase isoform, TOAD64, enolase-gamma and aldolase C.

C Bulliard, R Zurbriggen, J Tornare, M Faty, Z Dastoor, J L Dreyer

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.7field-weighted citation impact, top 36% 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

14 citing papers in PubMed, 56 citations in OpenAlex.

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  8. Redox proteomics in some age-related neurodegenerative disorders or models thereof.NeuroRx : the journal of the American Society for Experimental NeuroTherapeutics · 2006
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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

6 authors at 1 institution in 1 country.

C BulliardDepartment of Biochemistry, University of Fribourg, CH-1700 Fribourg, Switzerland.
R Zurbriggen
J Tornare
M Faty
Z Dastoor
J L Dreyer
University of Fribourg · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NADH-dichlorophenol-indophenol oxidoreductases (PMOs) were purified from synaptic plasma membranes or synaptic vesicles (small recycling vesicles) from both bovine and rat brains and from a neuroblastoma cell line, NB41A3. Several isoforms could be identified in purified plasma membranes and vesicles. Purification of the enzyme activity involved protein extraction with detergents, (NH4)2SO4 precipitation, chromatography under stringent conditions and native PAGE. PMO activity could be attributed to a very tight complex of several proteins that could not be separated except by SDS/PAGE. SDS/PAGE resolved the purified complex into at least five proteins, which could be micro-sequenced and identified unambiguously as hsc70, TOAD64 and glyceraldehyde-3-phosphate dehydrogenase tightly associated with the brain-specific proteins aldolase C and enolase-gamma. Enzyme activity could be purified from both synaptic plasma membranes and recycling vesicles, yields being much greater from the latter source. Highly purified plasma membranes (prepared from a neuroblastoma cell line NB41A3 by iminobiotinylation of intact cells and affinity purification with avidin and anti-avidin antibodies under very stringent conditions) also displayed PMO activity tightly associated with TOAD64. The association of PMO in a tight complex was confirmed by its immunoprecipitation from cellular and membrane extracts of NB41A3 using antibodies directed against any component protein of the complex followed by immunodetection with antibodies directed against the other members. Antibodies also inhibited the enzyme activity synergistically. In addition, induction of the different components of the complex during dichlorophenol-indophenol stress was demonstrated by the S1 RNase-protection assay in synchronized NB41A3 cells. The role of the complex in membrane fusion and cellular response to extracellular oxidative stress during growth and development is discussed.

Indexed as

Amino Acid SequenceAnimalsCattleElectrophoresis, Polyacrylamide GelFructose-Bisphosphate AldolaseGlyceraldehyde-3-Phosphate DehydrogenasesHSP70 Heat-Shock ProteinsIsoenzymesMacromolecular SubstancesMembrane ProteinsMolecular Sequence DataNADH, NADPH OxidoreductasesNeoplasm ProteinsNerve Tissue ProteinsNeuroblastomaOxidative Stressdichlorophenolindophenol reductaseFructose-Bisphosphate AldolaseGlyceraldehyde-3-Phosphate DehydrogenasesHSP70 Heat-Shock ProteinsIsoenzymesMacromolecular SubstancesMembrane ProteinsNADH, NADPH OxidoreductasesNeoplasm ProteinsNerve Tissue ProteinsPhosphopyruvate HydrataseQuinone Reductases

Identifiers

PMID9182718
PMCPMC1218466
OpenAlexW2108064744

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.