Evidence map›Paper›PMID 27845784›Full record

ArticleThe Analyst2016

Antibody purification via affinity membrane chromatography method utilizing nucleotide binding site targeting with a small molecule.

Nur Mustafaoglu, Tanyel Kiziltepe, Basar Bilgicer

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

Article in The Analyst, 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
0.6field-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

9 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Current advances in separation chemistry for antibody purification and analysis.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025
    Review
  3. Review
  4. Recent development and application of membrane chromatography.Analytical and bioanalytical chemistry · 2023
    Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Designer covalent heterobivalent inhibitors prevent IgE-dependent responses to peanut allergen.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

3 authors at 2 institutions in 2 countries.

Nur MustafaogluDepartment of Chemical and Biomolecular Engineering, University of Notre Dame, University of Notre Dame, Notre Dame, IN, USA.
Tanyel KiziltepeDepartment of Chemical and Biomolecular Engineering, University of Notre Dame, University of Notre Dame, Notre Dame, IN, USA and Advanced Diagnostics and Therapeutics, University of Notre Dame, University of Notre Dame, Notre Dame, IN, USA.
Basar BilgicerDepartment of Chemical and Biomolecular Engineering, University of Notre Dame, University of Notre Dame, Notre Dame, IN, USA and Advanced Diagnostics and Therapeutics, University of Notre Dame, University of Notre Dame, Notre Dame, IN, USA and Department of Chemistry and Biochemistry, University of Notre Dame, University of Notre Dame, Notre Dame, IN, USA and Mike and Josie Harper Cancer Research Institute, University of Notre Dame, University of Notre Dame, Notre Dame, IN, USA and Center for Rare & Neglected Diseases, University of Notre Dame, University of Notre Dame, Notre Dame, IN, USA. bbilgicer@nd.edu.
University of Notre Dame · USNotre Dame of Dadiangas University · PH

Funding

Designing Selective Inhibitors of IgE-mediated Mast Cell DegranulationR01AI108884 · NIAID · UNIVERSITY OF NOTRE DAME · PI BILGICER, ZIHNI BASAR · 2015 to 2024
$3.6M
NIAID NIH HHS R01 AI108884
6 · The paper itself

Abstract

Here, we present an affinity membrane chromatography technique for purification of monoclonal and polyclonal antibodies from cell culture media of hybridomas and ascites fluids. The m-NBST method utilizes the nucleotide-binding site (NBS) that is located on the Fab variable domain of immunoglobulins to enable capturing of antibody molecules on a membrane affinity column via a small molecule, tryptamine, which has a moderate binding affinity to the NBS. Regenerated cellulose membrane was selected as a matrix due to multiple advantages over traditionally used resin-based affinity systems. Rituximab was used for proof of concept experiments. Antibody purification was accomplished by first capture of injected samples while running equilibration buffer (50 mM sodium phosphate pH 7.0), followed by elution achieved by running a gradient of mild elution buffer (3 M NaCl in 50 mM phosphate pH 7.0). The results indicate that the m-NBST column efficiency for Rituximab was >98%, with a purity level of >98%. The quality and the capacity of this small molecule membrane affinity purification method is further evaluated for a number of parameters such as: injection concentrations, volumes, wash/bind time, elution gradient, antibody/protein-contaminant combinations, effects of injection buffer, post-purification antigen binding activity of antibodies, and column reusability and stability.

Indexed as

Chromatography, AffinityAnimalsAntigensBinding SitesMiceNucleotidesRituximabTryptaminesAntigensNucleotidesRituximabtryptamineTryptamines

Identifiers

PMID27845784
PMCPMC5245175
OpenAlexW2550969029

What OpenQuestion holds

Textmetadata
LicenceTDM
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.