Evidence map›Paper›PMID 27081368›Full record

ArticleSaudi journal of biological sciences2016

Optimization of expression and purification of HSPA6 protein from Camelus dromedarius in E. coli.

Ajamaluddin Malik, Abdulrahman M Alsenaidy, Mohamed Elrobh, Wajahatullah Khan, Mohammed S Alanazi, Mohammad D Bazzi

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Saudi journal of biological sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

9 citing papers in PubMed, 34 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

6 authors at 3 institutions in 2 countries.

Ajamaluddin MalikProtein Research Chair, Department of Biochemistry, College of Science, King Saud University, PO Box 2455, Riyadh 11451, Saudi Arabia.
Abdulrahman M AlsenaidyProtein Research Chair, Department of Biochemistry, College of Science, King Saud University, PO Box 2455, Riyadh 11451, Saudi Arabia.
Mohamed ElrobhGenome Research Chair, Department of Biochemistry, College of Science, King Saud University, PO Box 2455, Riyadh 11451, Saudi Arabia; Biochemistry Department, Faculty of Science, Ain-Shams University, Abbassia 11381, Cairo, Egypt.
Wajahatullah KhanDepartment of Basic Sciences, College of Science and Health Professions, King Saud Bin Abdulaziz University for Health Sciences, PO Box 3660, Riyadh 11426, Saudi Arabia.
Mohammed S AlanaziGenome Research Chair, Department of Biochemistry, College of Science, King Saud University, PO Box 2455, Riyadh 11451, Saudi Arabia.
Mohammad D BazziProtein Research Chair, Department of Biochemistry, College of Science, King Saud University, PO Box 2455, Riyadh 11451, Saudi Arabia; Genome Research Chair, Department of Biochemistry, College of Science, King Saud University, PO Box 2455, Riyadh 11451, Saudi Arabia.
King Saud University · SAAin Shams University · EGKing Saud bin Abdulaziz University for Health Sciences · SA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The HSPA6, one of the members of large family of HSP70, is significantly up-regulated and has been targeted as a biomarker of cellular stress in several studies. Herein, conditions were optimized to increase the yield of recombinant camel HSPA6 protein in its native state, primarily focusing on the optimization of upstream processing parameters that lead to an increase in the specific as well as volumetric yield of the protein. The results showed that the production of cHSPA6 was increased proportionally with increased incubation temperature up to 37 °C. Induction with 10 μM IPTG was sufficient to induce the expression of cHSPA6 which was 100 times less than normally used IPTG concentration. Furthermore, the results indicate that induction during early to late exponential phase produced relatively high levels of cHSPA6 in soluble form. In addition, 5 h of post-induction incubation was found to be optimal to produce folded cHSPA6 with higher specific and volumetric yield. Subsequently, highly pure and homogenous cHSPA6 preparation was obtained using metal affinity and size exclusion chromatography. Taken together, the results showed successful production of electrophoretically pure recombinant HSPA6 protein from Camelus dromedarius in Escherichia coli in milligram quantities from shake flask liquid culture.

Indexed as

2× LB, double strength Luria–Bertaniamp, ampicillinDTT, dithiothreitolEDTA, ethylenediaminetetraacetic acidExpression optimizationFast protein liquid chromatographyFPLC, fast protein liquid chromatographyHeat shock proteinHsp70IPTG, isopropyl β-d-1-thiogalactopyranosideLB, Luria–BertaniMolecular chaperoneNB, nutrient brothNi–NTA, nickel–nitrilotriacetic acidOD600, optical density at 600 nmPMSF, phenylmethylsulfonyl fluorideRecombinantrpm, rotations per minuteTB, terrific broth

Identifiers

PMID27081368
PMCPMC4818323
OpenAlexW2001737483

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.