Evidence map›Paper›PMID 30446961›Full record

ArticleMolecular biology reports2019

L-Asparaginase from Erwinia carotovora: insights about its stability and activity.

Marcele Faret, Stephanie Bath de Morais, Nilson Ivo Tonin Zanchin, Tatiana de Arruda Campos Brasil de Souza

Abstract read
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In one paragraph

Article in Molecular biology reports, 2019. 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
0.5field-weighted citation impact, top 28% 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, 4 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

4 authors at 1 institution in 1 country.

Marcele FaretInstituto Carlos Chagas, ICC - FIOCRUZ/PR, Rua Algacyr Munhoz Mader, 3775, bloco C, Curitiba,, Paraná, 81350-010, Brazil.
Stephanie Bath de MoraisInstituto Carlos Chagas, ICC - FIOCRUZ/PR, Rua Algacyr Munhoz Mader, 3775, bloco C, Curitiba,, Paraná, 81350-010, Brazil.
Nilson Ivo Tonin ZanchinInstituto Carlos Chagas, ICC - FIOCRUZ/PR, Rua Algacyr Munhoz Mader, 3775, bloco C, Curitiba,, Paraná, 81350-010, Brazil.
Tatiana de Arruda Campos Brasil de SouzaInstituto Carlos Chagas, ICC - FIOCRUZ/PR, Rua Algacyr Munhoz Mader, 3775, bloco C, Curitiba,, Paraná, 81350-010, Brazil. tatianabrasil@fiocruz.br.ORCID http://orcid.org/0000-0002-1850-6080
Fundação Carlos Chagas · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymatic prospection indicated that L-asparaginase from Erwinia carotovora (ECAR-LANS) posses low glutaminase activity and much effort has been made to produce therapeutic ECAR-LANS. However, its low stability precludes its use in therapy. Herein, biochemical and biophysical assays provided data highlighting the influence of solubilization and storage into ECAR-LANS structure, stability, and activity. Moreover, innovations in recombinant expression and purification guaranteed the purification of functional tetramers. According to solubilization condition, the L-asparaginase activity and temperature of melting ranged up to 25-32%, respectively. CD spectra indicate the tendency of ECAR-LANS to instability and the influence of β-structures in activity. These results provide relevant information to guide formulations with prolonged action in the bloodstream.

Indexed as

AsparaginaseCytoplasmEnzyme StabilityFluorescencePectobacterium carotovorumPeriplasmAsparaginaseBiophysical behaviorIn solution characterizationL-asparaginase

Identifiers

PMID30446961
OpenAlexW2900779921

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.