Evidence map›Paper›PMID 27282622›Full record

ArticleMolecular biotechnology2016

Purification and Characterization of Recombinant Darbepoetin Alfa from Leishmania tarentolae.

Anvarsadat Kianmehr, Abdolkarim Mahrooz, Morteza Oladnabi, Yaghoub Safdari, Javad Ansari, Kamal Veisi, Mehdi Evazalipour, Hamid Shahbazmohammadi, Eskandar Omidinia

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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 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 96% 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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. Recombinant Protein Drugs: A 2025 Update.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026
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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

9 authors at 7 institutions in 1 country.

Anvarsadat KianmehrBiochemistry & Metabolic Disorders Research Center, Golestan University of Medical Sciences, Gorgan, Iran.
Abdolkarim MahroozImmunogenetic Research Center, Mazandaran University of Medical Sciences, Sari, Iran.
Morteza OladnabiCongenital Malformations Research Center, Golestan University of Medical Sciences, Gorgan, Iran.
Yaghoub SafdariMedical Cellular and Molecular Research Center, Golestan University of Medical Sciences, Gorgan, Iran.
Javad AnsariCellular and Molecular Research Center, Qazvin University of Medical Sciences, Qazvin, Iran.
Kamal VeisiBiotechnology Department, School of Advanced Technologies in Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
Mehdi EvazalipourDepartment of Pharmaceutical Biotechnology, School of Pharmacy, Guilan University of Medical Sciences, Rasht, Iran.
Hamid ShahbazmohammadiEnzyme Technology Laboratory, Biochemistry Department, Metabolic and Genetic Research Group, Pasteur Institute of Iran, Tehran, Iran. hamidbiozyme@gmail.com.
Eskandar OmidiniaEnzyme Technology Laboratory, Biochemistry Department, Metabolic and Genetic Research Group, Pasteur Institute of Iran, Tehran, Iran. eomid8@yahoo.com.
Golestan University of Medical Sciences · IRPasteur Institute of Iran · IRGolestan University · IRGuilan University of Medical Sciences · IRMazandaran University of Medical Sciences · IRQazvin University of Medical Sciences · IRShahid Beheshti University of Medical Sciences · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Darbepoetin alfa is a biopharmaceutical glycoprotein that stimulates erythropoiesis and is used to treat anemia, which associated with renal failure and cancer chemotherapy. We herein describe the structural characterization of recombinant darbepoetin alfa produced by Leishmania tarentolae T7-TR host. The DNA expression cassette was integrated into the L. tarentolae genome through homologous recombination. Transformed clones were selected by antibiotic resistance, diagnostic PCRs, and protein expression analysis. The structure of recombinant darbepoetin alfa was analyzed by isoelectric focusing, ultraviolet-visible spectrum, and circular dichroism (CD) spectroscopy. Expression analysis showed the presence of a protein band at 40 kDa, and its expression level was 51.2 mg/ml of culture medium. Darbepoetin alfa have 5 isoforms with varying degree of sialylation. The UV absorption and CD spectra were analogous to original drug (Aranesp), which confirmed that the produced protein was darbepoetin alfa. Potency test results revealed that the purified protein was biologically active. In brief, the structural and biological characteristics of expressed darbepoetin alfa were very similar to Aranesp which has been normally expressed in CHO. Our data also suggest that produced protein has potential to be developed for clinical use.

Indexed as

Circular DichroismCloning, MolecularDarbepoetin alfaLeishmaniaMolecular WeightProtein IsoformsRecombinant ProteinsDarbepoetin alfaProtein IsoformsRecombinant ProteinsCharacterizationDarbepoetin alfaLeishmania tarentolaePurification

Identifiers

PMID27282622
OpenAlexW2416130024

What OpenQuestion holds

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Read underepoch 390

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.