Evidence map›Paper›PMID 18587671›Full record

ArticleMolecular and cellular biochemistry2009

Identification, purification, and characterization of a secretory serine protease in an Indian strain of Leishmania donovani.

Rajdeep Choudhury, Siddhartha Kumar Bhaumik, Tripti De, Tapati Chakraborti

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In one paragraph

Article in Molecular and cellular biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

2 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
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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

4 authors at 2 institutions in 1 country.

Rajdeep ChoudhuryDepartment of Biochemistry and Biophysics, University of Kalyani, Kalyani, West Bengal 741235, India.
Siddhartha Kumar Bhaumik
Tripti De
Tapati Chakraborti
Indian Institute of Chemical Biology · INUniversity of Kalyani · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An aprotinin sensitive serine protease was identified in the culture supernatant of the Indian strain of Leishmania donovani (MHOM/IN/1983/AG83). The protease was subsequently purified and characterized. The apparent molecular mass of the enzyme was 115 kDa in SDS-PAGE under non-reducing condition, while on reduction it showed a 56 kDa protein band indicating that the protease is a dimeric protein. The purified enzyme was optimally active at the pH and temperature of 7.5 and 28 degrees C, respectively. Assays of thermal stability indicated that the enzyme preserved 59% of activity even after pretreatment at 42 degrees C for 1 h. The purified protease was not glycosylated and its isoelectric pI was 5.0. N-alpha-p-tosyl-L-arginine methylester (TAME) appeared to be relatively better substrate among the commonly used synthetic substrates. The enzyme was inhibited by Ca(2+) and Mn(2+), but activated by Zn(2+). The protease could play important role(s) in the pathogenesis of visceral leishmaniasis or kala-azar.

Indexed as

Protozoan ProteinsSerine ProteasesAnimalsCations, DivalentEnzyme StabilityGlycosylationHumansHydrogen-Ion ConcentrationIndiaIsoelectric PointLeishmania donovaniMetalsSerine Proteinase InhibitorsSubstrate SpecificityTemperatureCations, DivalentMetalsProtozoan ProteinsSerine ProteasesSerine Proteinase Inhibitors

Identifiers

PMID18587671
OpenAlexW1965085707

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.