Evidence map›Paper›PMID 18975072›Full record

ArticleGlycoconjugate journal2009

The unique enzymatic function of field bean (Dolichos lablab) D-galactose specific lectin: a polyphenol oxidase.

Santosh R Kanade, Devavratha H Rao, Ramanath N Hegde, Lalitha R Gowda

Abstract read
PubMed Publisher
In one paragraph

Article in Glycoconjugate journal, 2009. 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
0.9field-weighted citation impact, top 18% 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, 9 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

4 authors at 2 institutions in 1 country.

Santosh R KanadeDepartment of Protein Chemistry and Technology, Central Food Technological Research Institute, Council of Scientific and Industrial Research (CSIR), Mysore, India.
Devavratha H Rao
Ramanath N Hegde
Lalitha R Gowda
Council of Scientific and Industrial Research · INCentral Food Technological Research Institute · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The polyphenol oxidase (PPO) of field bean (Dolichos lablab) is a tetramer made up of two subunits of mass 29,000 and 31,000 Da. The amino acid sequence of the tryptic peptides showed approximately 90% sequence identity to the D: -galactose specific legume lectins. The haemagglutinating activity of a pure and homogenous preparation of PPO measured using human erythrocytes was 1261 HAU mg(-1) protein and was inhibited by D: -galactose. Purification by galactose-sepharose chromatography also indicated that the PPO and haemagglutinating activities were associated with a single protein. Crude extracts of other legumes did not exhibit PPO activity, yet cross reacted with anti-PPO antibodies. This dual function protein with PPO and haemagglutinating activity is unique to field bean. The two activities are independent of each other occurring at different loci on the protein. These observations further evidence and strengthen the assumption that galactose specific legume lectins have enzymatic function. Both PPO and lectins are proteins that play a vital role in the defense mechanism of plants. The complementarity of these two simultaneous and independent powerful defense mechanisms exhibited by a single protein renders it a candidate gene for the development of inbuilt plant protection.

Indexed as

Catechol OxidaseChromatography, AffinityChromatography, GelDolichosElectrophoresis, Polyacrylamide GelErythrocytesGalactoseHumansPlant LectinsCatechol OxidaseGalactosePlant Lectins

Identifiers

PMID18975072
OpenAlexW2089513714

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.