Evidence map›Paper›PMID 16668546›Full record

ArticlePlant physiology1991

Immunological characterization of two dominant tonoplast polypeptides.

M Betz, K J Dietz

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 1991. 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
3.1field-weighted citation impact, top 9% 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, 28 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

2 authors at 1 institution in 1 country.

M BetzInstitut für Botanik und Pharmazeutische Biologie, Julius-Maximilians-Universität Würzburg, Mittlerer Dallenbergweg 64, 8700 Würzburg, Germany.
K J Dietz
University of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

At least 14 distinct polypeptides reside in the tonoplast of barley (Hordeum vulgare) mesophyll vacuoles. Two of the polypeptides were isolated from two-dimensional separations of vacuoplast membrane proteins and used for immunization. With the antisera, the localization on the membrane and the distribution of the polypeptides in the plant kingdom and in various tissues of barley plants was studied. The polypeptides have an apparent molecular mass of 31 and 40 kilodaltons. After freeze-thaw cycles or washing of the membranes with 4.5 millimolar NaCl, the polypeptides were still sedimented with the membranes, suggesting an intrinsic localization. The antiserum against the 31-kilodalton polypeptide bound to the outer surface of isolated intact vacuoles. In chromatographic separations of Triton X-100-solubilized membrane fractions, the residual activities of various acid hydrolases eluted distinct from the 31- and 40-kilodalton polypeptides. Both polypeptides tend to form larger aggregates, however smaller than the tonoplast ATPase. Cross-reactive polypeptides were present in higher and lower plants (the green alga Chara corallina and the liverwort Conocephalum) and in liver tissue from rat and beef, but were not detected in other animal tissues tested so far. The results indicate a wide distribution of these tonoplast polypeptides in vacuole-containing organisms.

Identifiers

PMID16668546
PMCPMC1081161
OpenAlexW2065369590

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.