Evidence map›Paper›PMID 31375727›Full record

ArticleScientific reports2019

Rapid affinity chromatographic isolation method for LDL in human plasma by immobilized chondroitin-6-sulfate and anti-apoB-100 antibody monolithic disks in tandem.

Thanaporn Liangsupree, Evgen Multia, Jari Metso, Matti Jauhiainen, Patrik Forssén, Torgny Fornstedt, Katariina Öörni, Aleš Podgornik, Marja-Liisa Riekkola

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

11 citing papers in PubMed, 21 citations in OpenAlex.

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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 5 institutions in 3 countries.

Thanaporn LiangsupreeDepartment of Chemistry, University of Helsinki, P.O. Box 55, FI-00014, Helsinki, Finland.ORCID http://orcid.org/0000-0003-0431-2186
Evgen MultiaDepartment of Chemistry, University of Helsinki, P.O. Box 55, FI-00014, Helsinki, Finland.ORCID http://orcid.org/0000-0002-8717-8842
Jari MetsoMinerva Foundation Institute for Medical Research and National Institute for Health and Welfare, Biomedicum 2U, Helsinki, Finland.
Matti JauhiainenMinerva Foundation Institute for Medical Research and National Institute for Health and Welfare, Biomedicum 2U, Helsinki, Finland.
Patrik ForssénDepartment of Engineering and Chemical Sciences, Karlstad University, SE-651 88, Karlstad, Sweden.
Torgny FornstedtDepartment of Engineering and Chemical Sciences, Karlstad University, SE-651 88, Karlstad, Sweden.
Katariina ÖörniWihuri Research Institute, Atherosclerosis Research Laboratory, Haartmaninkatu 8, 00290, Helsinki, Finland.ORCID http://orcid.org/0000-0002-9525-0250
Aleš PodgornikFaculty of Chemistry and Chemical Technology, University of Ljubljana, Ljubljana, Slovenia.
Marja-Liisa RiekkolaDepartment of Chemistry, University of Helsinki, P.O. Box 55, FI-00014, Helsinki, Finland. marja-liisa.riekkola@helsinki.fi.ORCID http://orcid.org/0000-0001-7519-9892
University of Helsinki · FIKarlstad University · SEMinerva Foundation · FIUniversity of Ljubljana · SIWihuri Research Institute · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Low-density lipoprotein (LDL) is considered the major risk factor for the development of atherosclerotic cardiovascular diseases (ASCVDs). A novel and rapid method for the isolation of LDL from human plasma was developed utilising affinity chromatography with monolithic stationary supports. The isolation method consisted of two polymeric monolithic disk columns, one immobilized with chondroitin-6-sulfate (C6S) and the other with apolipoprotein B-100 monoclonal antibody (anti-apoB-100 mAb). The first disk with C6S was targeted to remove chylomicrons, very-low-density lipoprotein (VLDL) particles, and their remnants including intermediate-density lipoprotein (IDL) particles, thus allowing the remaining major lipoprotein species, i.e. LDL, lipoprotein(a) (Lp(a)), and high-density lipoprotein (HDL) to flow to the anti-apoB-100 disk. The second disk captured LDL particles via the anti-apoB-100 mAb attached on the disk surface in a highly specific manner, permitting the selective LDL isolation. The success of LDL isolation was confirmed by different techniques including quartz crystal microbalance. In addition, the method developed gave comparable results with ultracentrifugation, conventionally used as a standard method. The reliable results achieved together with a short isolation time (less than 30 min) suggest the method to be suitable for clinically relevant LDL functional assays.

Indexed as

Antibodies, ImmobilizedAntibodies, MonoclonalApolipoprotein B-100Chondroitin SulfatesChromatography, AffinityChylomicronsHumansLipoproteins, LDLTime FactorsAntibodies, ImmobilizedAntibodies, MonoclonalApolipoprotein B-100Chondroitin SulfatesChylomicronsLipoproteins, LDL

Identifiers

PMID31375727
PMCPMC6677805
OpenAlexW2964897832

What OpenQuestion holds

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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.