Evidence map›Paper›PMID 24751557›Full record

ArticleJournal of chromatography. A2014

High ionic strength narrows the population of sites participating in protein ion-exchange adsorption: a single-molecule study.

Lydia Kisley, Jixin Chen, Andrea P Mansur, Sergio Dominguez-Medina, Eliona Kulla, Marci K Kang, Bo Shuang, Katerina Kourentzi, Mohan-Vivekanandan Poongavanam, Sagar Dhamane and 2 more

Abstract read
In one paragraph

Article in Journal of chromatography. A, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. A mechanistic examination of salting out in protein-polymer membrane interactions.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  5. Article
  6. Article
  7. Review
  8. Review
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

12 authors.

Lydia KisleyDepartment of Chemistry, Rice University, Houston, TX 77251, USA. Electronic address: lk12@rice.edu.
Jixin ChenDepartment of Chemistry, Rice University, Houston, TX 77251, USA. Electronic address: Jixin.chen@rice.edu.
Andrea P MansurDepartment of Chemistry, Rice University, Houston, TX 77251, USA. Electronic address: andrea.p.mansur@rice.edu.
Sergio Dominguez-MedinaDepartment of Chemistry, Rice University, Houston, TX 77251, USA. Electronic address: Sergio.Dominguez-Medina@rice.edu.
Eliona KullaDepartment of Chemistry, Rice University, Houston, TX 77251, USA. Electronic address: Eliona.Kulla@rice.edu.
Marci K KangDepartment of Chemistry, Rice University, Houston, TX 77251, USA. Electronic address: Marci.Kang@rice.edu.
Bo ShuangDepartment of Chemistry, Rice University, Houston, TX 77251, USA. Electronic address: bs16@rice.edu.
Katerina KourentziDepartment of Chemical & Biomolecular Engineering, University of Houston, Houston, TX 77004, USA. Electronic address: edkourentzi@uh.edu.
Mohan-Vivekanandan PoongavanamDepartment of Biology & Biochemistry, University of Houston, Houston, TX 77004, USA. Electronic address: mohan.vivekanandha@gmail.com.
Sagar DhamaneDepartment of Biology & Biochemistry, University of Houston, Houston, TX 77004, USA. Electronic address: dhamane.edu@gmail.com.
Richard C WillsonDepartment of Chemical & Biomolecular Engineering, University of Houston, Houston, TX 77004, USA; Department of Biology & Biochemistry, University of Houston, Houston, TX 77004, USA; Houston Methodist Research Institute, Houston, TX 77030, USA; Centro de Biotecnología FEMSA, Departamento de Biotecnología e Ingeniería de Alimentos, Tecnológico de Monterrey, Monterrey NL 64849, Mexico. Electronic address: willson@uh.edu.
Christy F LandesDepartment of Chemistry, Rice University, Houston, TX 77251, USA; Department of Electrical and Computer Engineering, Rice University, Houston, TX 77251, USA. Electronic address: cflandes@rice.edu.

Funding

Structure and Function of NMDA ReceptorsR01GM094246 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI JAYARAMAN, VASANTHI · 2011 to 2016
$2.0M
NIGMS NIH HHS GM94246-01A1NIGMS NIH HHS R01 GM094246
6 · The paper itself

Abstract

The retention and elution of proteins in ion-exchange chromatography is routinely controlled by adjusting the mobile phase salt concentration. It has repeatedly been observed, as judged from adsorption isotherms, that the apparent heterogeneity of adsorption is lower at more-eluting, higher ionic strength. Here, we present an investigation into the mechanism of this phenomenon using a single-molecule, super-resolution imaging technique called motion-blur Points Accumulation for Imaging in Nanoscale Topography (mbPAINT). We observed that the number of functional adsorption sites was smaller at high ionic strength and that these sites had reduced desorption kinetic heterogeneity, and thus narrower predicted elution profiles, for the anion-exchange adsorption of α-lactalbumin on an agarose-supported, clustered-charge ligand stationary phase. Explanations for the narrowing of the functional population such as inter-protein interactions and protein or support structural changes were investigated through kinetic analysis, circular dichroism spectroscopy, and microscopy of agarose microbeads, respectively. The results suggest the reduction of heterogeneity is due to both electrostatic screening between the protein and ligand and tuning the steric availability within the agarose support. Overall, we have shown that single molecule spectroscopy can aid in understanding the influence of ionic strength on the population of functional adsorbent sites participating in the ion-exchange chromatographic separation of proteins.

Indexed as

AdsorptionChromatography, Ion ExchangeCircular DichroismKineticsLactalbuminLigandsOsmolar ConcentrationProteinsSepharoseLactalbuminLigandsProteinsSepharoseBioseparationsHeterogeneityIon-exchangembPAINTOptical nanoscopy

Identifiers

PMID24751557
PMCPMC4035562

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.