Evidence map›Paper›PMID 24336509›Full record

ArticleScientific reports2013

Integrated enzyme reactor and high resolving chromatography in "sub-chip" dimensions for sensitive protein mass spectrometry.

Hanne Kolsrud Hustoft, Ole Kristian Brandtzaeg, Magnus Rogeberg, Dorna Misaghian, Silje Bøen Torsetnes, Tyge Greibrokk, Léon Reubsaet, Steven Ray Wilson, Elsa Lundanes

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In one paragraph

Article in Scientific reports, 2013. 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
–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

11 citing papers in PubMed.

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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.

Hanne Kolsrud HustoftDepartment of Chemistry, University of Oslo, Post Box 1033 Blindern, NO-0315 Oslo, Norway.
Ole Kristian BrandtzaegDepartment of Chemistry, University of Oslo, Post Box 1033 Blindern, NO-0315 Oslo, Norway.
Magnus Rogeberg1] Department of Chemistry, University of Oslo, Post Box 1033 Blindern, NO-0315 Oslo, Norway [2] Department of Neurology, Akershus University Hospital, 1478 Lørenskog, Norway.
Dorna MisaghianDepartment of Chemistry, University of Oslo, Post Box 1033 Blindern, NO-0315 Oslo, Norway.
Silje Bøen TorsetnesSchool of Pharmacy, University of Oslo, Post Box 1068 Blindern, NO-0316 Oslo, Norway.
Tyge GreibrokkDepartment of Chemistry, University of Oslo, Post Box 1033 Blindern, NO-0315 Oslo, Norway.
Léon ReubsaetSchool of Pharmacy, University of Oslo, Post Box 1068 Blindern, NO-0316 Oslo, Norway.
Steven Ray WilsonDepartment of Chemistry, University of Oslo, Post Box 1033 Blindern, NO-0315 Oslo, Norway.
Elsa LundanesDepartment of Chemistry, University of Oslo, Post Box 1033 Blindern, NO-0315 Oslo, Norway.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reliable, sensitive and automatable analytical methodology is of great value in e.g. cancer diagnostics. In this context, an on-line system for enzymatic cleavage of proteins, subsequent peptide separation by liquid chromatography (LC) with mass spectrometric detection has been developed using "sub-chip" columns (10-20 μm inner diameter, ID). The system could detect attomole amounts of isolated cancer biomarker progastrin-releasing peptide (ProGRP), in a more automatable fashion compared to previous methods. The workflow combines protein digestion using an 20 μm ID immobilized trypsin reactor with a polymeric layer of 2-hydroxyethyl methacrylate-vinyl azlactone (HEMA-VDM), desalting on a polystyrene-divinylbenzene (PS-DVB) monolithic trap column, and subsequent separation of resulting peptides on a 10 μm ID (PS-DVB) porous layer open tubular (PLOT) column. The high resolution of the PLOT columns was maintained in the on-line system, resulting in narrow chromatographic peaks of 3-5 seconds. The trypsin reactors provided repeatable performance and were compatible with long-term storage.

Indexed as

Enzymes, ImmobilizedProteomicsBiomarkersChromatography, LiquidHumansMass SpectrometryNanotechnologyPeptide FragmentsRecombinant ProteinsTrypsinBiomarkersEnzymes, ImmobilizedPeptide Fragmentspro-gastrin-releasing peptide (31-98)Recombinant ProteinsTrypsin

Identifiers

PMID24336509
PMCPMC3863811

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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.