Characterization of Syrian hamster gastric mucosal H+,K+-ATPase.

P K Chatterjee, P K Das

Abstract read

In one paragraph

Article in Molecular and cellular biochemistry, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

–field-weighted citation impact, top 92% 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

0 citing papers in PubMed, 3 citations in OpenAlex.

No citing paper in PubMed yet.

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 1 institution in 1 country.

P K ChatterjeeIndian Institute of Chemical Biology, Calcutta, India.

P K Das

Indian Institute of Chemical Biology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Employing a simple one-step sucrose gradient fractionation method, gastric mucosal membrane of Syrian hamster was prepared and demonstrated to be specifically enriched in H+,K+-ATPase activity. The preparation is practically devoid of other ATP hydrolyzing activity and contains high K+-stimulated ATPase activity of at least 4-5 fold compared to basal ATPase activity. The H+,K+-ATPase showed hydroxylamine-sensitive phosphorylation and K+-dependent dephosphorylation of the phosphoenzyme, characteristic inhibition by vanadate, omeprazole and SCH 28080, and nigericin-reversible K+-dependent H+-transport--properties characteristic of gastric proton pump. One notable difference with H+,K+-ATPase of other species has been the observation of valinomycin-independent H+ transport in such membrane vesicles. It is proposed that such H+,K+-ATPase-rich hamster gastric mucosal membrane preparation might provide a unique model to study physiological aspects of H+,K+-ATPase function in relation to HCl secretion.

Indexed as

Adenosine TriphosphateAnimalsAnti-Ulcer AgentsCricetinaeEnzyme InhibitorsFemaleGastric AcidGastric MucosaH(+)-K(+)-Exchanging ATPaseImidazolesMaleMesocricetusNigericinOmeprazolePhosphorylationProton Pump InhibitorsAdenosine TriphosphateAnti-Ulcer AgentsEnzyme InhibitorsH(+)-K(+)-Exchanging ATPaseImidazolesNigericinOmeprazoleProton Pump InhibitorsProtonsSch 28080Vanadates

Identifiers

PMID8594424

DOI10.1007/BF00928146

OpenAlexW2021105109

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.