Evidence map›Paper›PMID 38338645›Full record

ArticleInternational journal of molecular sciences2024

Affinity Resins for the Isolation of Immunoglobulins G Obtained Using Biocatalytic Technology.

Mikhail N Tereshin, Tatiana D Melikhova, Barbara Z Eletskaya, Olga B Ksenofontova, Pavel V Pantyushenko, Maria Ya Berzina, Igor Ivanov, Igor V Myagkikh, Vasiliy N Stepanenko

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 39% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
  2. 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

9 authors at 2 institutions in 1 country.

Mikhail N TereshinShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya St. 16/10, 117437 Moscow, Russia.ORCID 0000-0002-8865-8223
Tatiana D MelikhovaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya St. 16/10, 117437 Moscow, Russia.
Barbara Z EletskayaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya St. 16/10, 117437 Moscow, Russia.ORCID 0000-0002-9552-7141
Olga B KsenofontovaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya St. 16/10, 117437 Moscow, Russia.
Pavel V PantyushenkoShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya St. 16/10, 117437 Moscow, Russia.ORCID 0009-0001-1466-9376
Maria Ya BerzinaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya St. 16/10, 117437 Moscow, Russia.ORCID 0000-0002-5684-8188
Igor IvanovLomonosov Institute of Fine Chemical Technologies, MIREA-Russian Technological University, Vernadskogo pr. 86, 119571 Moscow, Russia.ORCID 0000-0003-0543-2067
Igor V MyagkikhShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya St. 16/10, 117437 Moscow, Russia.
Vasiliy N StepanenkoShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya St. 16/10, 117437 Moscow, Russia.
Institute of Bioorganic Chemistry · RUMIREA - Russian Technological University · RU

Funding

«Greenvan» Limited Liability Company, Moscow, Russia no
6 · The paper itself

Abstract

Affinity chromatography resins that are obtained by conjugation of matrices with proteins of bacterial origin, like protein A, are frequently used for the purification of numerous therapeutic monoclonal antibodies. This article presents the development of a biocatalytic method for the production of novel affinity resins with an immobilized mutant form of protein A via sortase A mediated reaction. The conditions for activation of the agarose Seplife 6FF matrix, selection of different types of linkers with free amino groups and conditions for immobilization of recombinant protein A on the surface of the activated matrix were studied. Finally, the basic operational properties, like dynamic binding capacity (DBC), temperature dependance of DBC and stability during the cleaning-in-place process of the affinity resin with the Gly-Gly-EDA-Gly-Gly linker, were assessed using recombinant hyperchimeric monoclonal antibodies. The main characteristics show comparable results with the widely used commercial samples.

Indexed as

Antibodies, MonoclonalImmunoglobulin GChromatography, AffinityTechnologyAntibodies, MonoclonalImmunoglobulin Gmonoclonal antibodiesprotein A chromatographysortase A

Identifiers

PMID38338645
PMCPMC10855859
OpenAlexW4391137830

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.