Evidence map›Paper›PMID 40628978›Full record

ArticleAnalytical and bioanalytical chemistry2025

Protein pellet sample preparation for the analysis of N-glycans of therapeutic proteins.

Ronald L Kowle, Shardrack O Asare

Abstract read
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Article in Analytical and bioanalytical chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Ronald L KowleAnalytical Development, Bioproduct Research and Development, Eli Lilly and Company, 1223 W. Morris St, Indianapolis, IN, 46221, USA.
Shardrack O AsareAnalytical Development, Bioproduct Research and Development, Eli Lilly and Company, 1223 W. Morris St, Indianapolis, IN, 46221, USA. asare_shardrack@lilly.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Profiling of N-glycans of therapeutic proteins is a critical component in the control of biopharmaceutical products. N-Glycosylation, a common post-translational modification has been shown to impact the structure, function, stability, pharmacokinetics, and overall therapeutic efficacy of therapeutic proteins. Regulatory agencies around the world require detailed profiling of glycosylation to meet high product quality standards. The standard sample preparation for N-glycan analysis involves the enzymatic release of the glycan from the glycoprotein, fluorescent derivatization, and the time- and resource-consuming solid-phase extraction to remove excess fluorophore and reaction reagents before chromatographic glycan analysis. In this paper, we report a rapid sample preparation workflow that simplifies glycan purification after derivatization. The method uses the "protein pellet" approach to purify the fluorescently labeled glycan before analysis. The accuracy of the "protein pellet" method was established by comparing the results to the standard solid-phase extraction method that utilizes a polyamide stationary phase. The repeatability and linearity were also demonstrated.

Indexed as

GlycoproteinsPolysaccharidesProteinsGlycosylationHumansSolid Phase ExtractionGlycoproteinsPolysaccharidesProteinsGlycanHILICPelletProteinPurificationSPE

Identifiers

What OpenQuestion holds

Textmetadata
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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.