Evidence map›Paper›PMID 28555432›Full record

Article3 Biotech2017

Procoagulant serine glycoprotease from Cucumis sativus L.: action on human fibrinogen and fibrin clot.

Zohara Nafeesa, B R Shivalingu, K N Neema, Raghu Ram Achar, B K Venkatesh, Veeresh Hanchinal, B S Priya, S Nanjunda Swamy

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in 3 Biotech, 2017. 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
0.2field-weighted citation impact, top 41% 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, 7 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

8 authors at 3 institutions in 1 country.

Zohara NafeesaDepartment of Biotechnology, Sri Jayachamarajendra College of Engineering, JSS Science and Technology University, JSS Technical Institutions Campus, Mysuru, Karnataka, 570 006, India.
B R ShivalinguDepartment of Biotechnology, Sri Jayachamarajendra College of Engineering, JSS Science and Technology University, JSS Technical Institutions Campus, Mysuru, Karnataka, 570 006, India.
K N NeemaDepartment of Biotechnology, Sri Jayachamarajendra College of Engineering, JSS Science and Technology University, JSS Technical Institutions Campus, Mysuru, Karnataka, 570 006, India.
Raghu Ram AcharBiochemistry Division, Faculty of Life Sciences, JSS University, Mysore, Karnataka, 570 015, India.
B K VenkateshDepartment of Biotechnology, Sri Jayachamarajendra College of Engineering, JSS Science and Technology University, JSS Technical Institutions Campus, Mysuru, Karnataka, 570 006, India.
Veeresh HanchinalLiveon Biolabs Pvt. Ltd., Tumakuru, Karnataka, 572106, India.
B S PriyaDepartment of Studies in Chemistry, University of Mysore, Manasagangotri, Mysore, Karnataka, 570 006, India.
S Nanjunda SwamyDepartment of Biotechnology, Sri Jayachamarajendra College of Engineering, JSS Science and Technology University, JSS Technical Institutions Campus, Mysuru, Karnataka, 570 006, India. nanju_chem@yahoo.com.
JSS Science and Technology University · INJSS Academy of Higher Education and Research · INUniversity of Mysore · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Upon examination of the fruit extract of Cucumis sativus L. for its pharmacological benefits, it was previously observed that it has potential proteolytic, fibrinogenolytic and procoagulant activities. These properties can be attributed to the presence of the protease. In this regard, the present study comprised of purification and characterization of protease. Purification of the enzyme involved ammonium sulfate precipitation followed by gel filtration and ion exchange chromatography. The purified cucumis protease (CPro) exhibits homogeneity as attested by SDS-PAGE and RP-HPLC with a retention time of 14.246 min with molecular mass ~75.3 kDa. CPro was identified as a glycoprotein and serine protease. Azocasein is the preferred substrate for CPro as it showed low K

Indexed as

Cucumis proteaseFibrin(ogen)olyticGlycoproteinHemostasisProcoagulantSerine protease

Identifiers

PMID28555432
PMCPMC5447519
OpenAlexW2619516957

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.