Evidence map›Paper›PMID 26322323›Full record

ArticleData in brief2015

Data set for mass spectrometric analysis of recombinant human serum albumin from various expression systems.

Daryl G S Smith, Grant E Frahm, Anita Kane, Barry Lorbetskie, Michel Girard, Michael J W Johnston, Terry D Cyr

Open access · goldAbstract read
In one paragraph

Article in Data in brief, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 99% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

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

7 authors at 1 institution in 1 country.

Daryl G S SmithCentre for Biologics Evaluation, Biologics and Genetic Therapies Directoriate, Health Canada, Ottawa, ON, Canada K1A0K9.
Grant E FrahmCentre for Biologics Evaluation, Biologics and Genetic Therapies Directoriate, Health Canada, Ottawa, ON, Canada K1A0K9.
Anita KaneCentre for Biologics Evaluation, Biologics and Genetic Therapies Directoriate, Health Canada, Ottawa, ON, Canada K1A0K9.
Barry LorbetskieCentre for Biologics Evaluation, Biologics and Genetic Therapies Directoriate, Health Canada, Ottawa, ON, Canada K1A0K9.
Michel GirardCentre for Biologics Evaluation, Biologics and Genetic Therapies Directoriate, Health Canada, Ottawa, ON, Canada K1A0K9.
Michael J W JohnstonCentre for Biologics Evaluation, Biologics and Genetic Therapies Directoriate, Health Canada, Ottawa, ON, Canada K1A0K9.
Terry D CyrCentre for Biologics Evaluation, Biologics and Genetic Therapies Directoriate, Health Canada, Ottawa, ON, Canada K1A0K9.
Health Canada · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human serum albumin (HSA) is a versatile and important protein for the pharmaceutical industry (Fanali et al., Mol. Aspects Med. 33(3) (2012) 209-290). Due to the potential transmission of pathogens from plasma sourced albumin, numerous expression systems have been developed to produce recombinant HSA (rHSA) (Chen et al., Biochim. Biophys. Acta (BBA)-Gen. Subj. 1830(12) (2013) 5515-5525; Kobayashi, Biologicals 34(1) (2006) 55-59). Based on our previous study showing increased glycation of rHSA expressed in Asian rice (Frahm et al., J. Phys. Chem. B 116(15) (2012) 4661-4670), both supplier-to-supplier and lot-to-lot variability of rHSAs from a number of expression systems were evaluated using reversed phase liquid chromatography linked with MS and MS/MS analyses. The data are associated with the research article 'Determination of Supplier-to-Supplier and Lot-to-Lot Variability in Glycation of Recombinant Human Serum Albumin Expressed in Oryza sativa' where further analysis of rHSA samples with additional biophysical methods can be found (Frahm et al., PLoS ONE 10(9) (2014) e109893). We determined that all rHSA samples expressed in rice showed elevated levels of arginine and lysine hexose glycation compared to rHSA expressed in yeast, suggesting that the extensive glycation of the recombinant proteins is a by-product of either the expression system or purification process and not a random occurrence.

Indexed as

AlbuminGlycationMass spectrometryOryza sativaRecombinant proteins

Identifiers

PMID26322323
PMCPMC4543087
OpenAlexW1064284836

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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.