Evidence map›Paper›PMID 35056992›Full record

ArticlePharmaceutics2022

Purification Process of a Recombinant Human Follicle Stimulating Hormone Biosimilar (Primapur

Maria Sinegubova, Ivan Vorobiev, Anatoly Klishin, Dmitry Eremin, Nadezhda Orlova, Natalya Orlova, Mikhail Polzikov

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

Article in Pharmaceutics, 2022. 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
1.0field-weighted citation impact, top 27% 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, 9 citations in OpenAlex.

  1. Article
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 2 institutions in 1 country.

Maria SinegubovaLaboratory of Mammalian Cell Bioengineering, Institute of Bioengineering, Federal State Institution «Federal Research Centre «Fundamentals of Biotechnology» of the Russian Academy of Sciences», Leninsky Prospect, 33, Build. 2, 119071 Moscow, Russia.ORCID 0000-0002-8950-6061
Ivan VorobievLaboratory of Mammalian Cell Bioengineering, Institute of Bioengineering, Federal State Institution «Federal Research Centre «Fundamentals of Biotechnology» of the Russian Academy of Sciences», Leninsky Prospect, 33, Build. 2, 119071 Moscow, Russia.ORCID 0000-0003-0064-4458
Anatoly KlishinState Research Institute of Genetics and Selection of Industrial Microorganisms of National Research Center «Kurchatov Institute», Dorozhniy Proezd, 1, 117545 Moscow, Russia.
Dmitry EreminIVFarma LLC, Nauchnyi Proezd, 20, Build. 2, 117246 Moscow, Russia.
Nadezhda OrlovaLaboratory of Mammalian Cell Bioengineering, Institute of Bioengineering, Federal State Institution «Federal Research Centre «Fundamentals of Biotechnology» of the Russian Academy of Sciences», Leninsky Prospect, 33, Build. 2, 119071 Moscow, Russia.ORCID 0000-0001-9483-2892
Natalya OrlovaState Research Institute of Genetics and Selection of Industrial Microorganisms of National Research Center «Kurchatov Institute», Dorozhniy Proezd, 1, 117545 Moscow, Russia.
Mikhail PolzikovIVFarma LLC, Nauchnyi Proezd, 20, Build. 2, 117246 Moscow, Russia.ORCID 0000-0001-5345-0230
Russian Academy of Sciences · RUKurchatov Institute · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recombinant human follicle stimulating hormone (r-hFSH) is widely used for infertility treatment and is subject to the development of biosimilars. There are different purification strategies that can yield r-hFSH of pharmaceutical quality from Chinese hamster ovary cell culture broth. We developed a purification process for r-hFSH centered on immunoaffinity chromatography with single-domain recombinant camelid antibodies. The resulting downstream process is simple and devoid of ultrafiltration operations. Studies on chromatography resin resource and ligand leakage showed that the immunoaffinity matrix employed was suitable for industrial use and stable for at least 40 full chromatography cycles, and the leaked single-domain antibody ligand was completely removed by subsequent purification steps. All chromatography resins employed withstood the same 40 cycles of use without significant changes in separation efficiency and product binding capacity. The resulting industrial purification process yielded batches of r-hFSH with consistent levels of purity and bioactivity.

Indexed as

batch-to-batch consistencybiopharmaceuticalsbiosimilarsdownstreamdynamic binding capacity (DBC)follitropin alphaimmunoaffinity chromatographyrecombinant human follicle stimulating hormone (r-hFSH)

Identifiers

PMID35056992
PMCPMC8781808
OpenAlexW4205368186

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.