Evidence map›Paper›PMID 26921192›Full record

ArticleMolecular biotechnology2016

Biochemical and in silico Characterization of Recombinant L-Lactate Dehydrogenase of Theileria annulata.

Belma Nural, Aysegul Erdemir, Ozal Mutlu, Sinem Yakarsonmez, Ozkan Danis, Murat Topuzogullari, Dilek Turgut-Balik

Abstract read
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Article in Molecular biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

4 citing papers in PubMed, 8 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

7 authors at 3 institutions in 1 country.

Belma NuralDepartment of Biotechnology and Biosafety, Institute of Science, Eskisehir Osmangazi University, Meselik, 26480, Eskisehir, Turkey.
Aysegul ErdemirDepartment of Bioengineering, Faculty of Chemical and Metallurgical Engineering, Yildiz Technical University, Davutpasa Campus, Esenler, 34210, Istanbul, Turkey.
Ozal MutluDepartment of Biology, Faculty of Arts and Sciences, Marmara University, Goztepe Campus, Goztepe, 34722, Istanbul, Turkey.
Sinem YakarsonmezDepartment of Bioengineering, Faculty of Chemical and Metallurgical Engineering, Yildiz Technical University, Davutpasa Campus, Esenler, 34210, Istanbul, Turkey.
Ozkan DanisDepartment of Chemistry, Faculty of Arts and Sciences, Marmara University, Goztepe Campus, Goztepe, 34722, Istanbul, Turkey.
Murat TopuzogullariDepartment of Bioengineering, Faculty of Chemical and Metallurgical Engineering, Yildiz Technical University, Davutpasa Campus, Esenler, 34210, Istanbul, Turkey.
Dilek Turgut-BalikDepartment of Bioengineering, Faculty of Chemical and Metallurgical Engineering, Yildiz Technical University, Davutpasa Campus, Esenler, 34210, Istanbul, Turkey. dilekbalik@gmail.com.
Yıldız Technical University · TRMarmara University · TREskişehir Osmangazi University · TR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Theileria annulata is a parasite that causes theileriosis in cattle. Reports about drug resistance made essential to develop new drug. LDH of Theileria schizonts is the vital enzyme for its anaerobic metabolism. TaLDH gene was first cloned into pGEM-T cloning vector with two introns in our previous study. Here we report cloning of TaLDH without introns into pLATE 31 vector in E. coli BL21(DE3). Protein was in an inactive form. Two mutations were fixed to express the active protein. Protein was purified by affinity chromatography and evaluated by SDS-PAGE and size exclusion chromatography. Optimum pH of enzyme was performed in pH 7.5, and enzyme was stabilized at 20-40 °C. Enzyme kinetics of recombinant TaLDH were found to be in the direction of pyruvate to lactate K m 0.1324 and K i 4.295 mM, k cat, 44.55/s and k cat /K m, 3.3693 × 10(5)/M/s. 3D structure of TaLDH was predicted, and possible drug binding sites were determined by homology modelling.

Indexed as

Binding SitesComputer SimulationEnzyme StabilityL-Lactate DehydrogenaseModels, MolecularMutationRecombinant ProteinsStructural Homology, ProteinTheileria annulataL-Lactate DehydrogenaseRecombinant ProteinsHomology modellingLDHSubstrate inhibitionTheileria annulataThermostability

Identifiers

PMID26921192
OpenAlexW2283905972

What OpenQuestion holds

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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.