Evidence map›Paper›PMID 41078838›Full record

ArticleACS omega2025

Complex Investigation of the Similarities and Differences between Ten Commercially Available Human Serum Albumin Preparations.

Rita Jakabfi-Csepregi, Zoltán Nagymihály, Zoltán Horváth-Szalai, Balázs Szirmay, Éva Varga-Visi, Omeralfaroug Ali, Edward Agyarko, András Szabó, Miklós Poór

Abstract read
In one paragraph

Article in ACS omega, 2025. 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
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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

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.

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

9 authors.

Rita Jakabfi-CsepregiDepartment of Laboratory Medicine, Medical School, University of Pécs, Ifjúság útja 13, Pécs H-7624, Hungary.
Zoltán NagymihályMolecular Medicine Research Group, János Szentágothai Research Centre, University of Pécs, Ifjúság útja 20, Pécs H-7624, Hungary.
Zoltán Horváth-SzalaiDepartment of Laboratory Medicine, Medical School, University of Pécs, Ifjúság útja 13, Pécs H-7624, Hungary.
Balázs SzirmayDepartment of Laboratory Medicine, Medical School, University of Pécs, Ifjúság útja 13, Pécs H-7624, Hungary.
Éva Varga-VisiAgribiotechnology and Precision Breeding for Food Security National Laboratory, Institute of Physiology and Nutrition, Department of Physiology and Animal Health, Hungarian University of Agriculture and Life Sciences, Guba Sándor u. 40, Kaposvár H-7400, Hungary.
Omeralfaroug AliAgribiotechnology and Precision Breeding for Food Security National Laboratory, Institute of Physiology and Nutrition, Department of Physiology and Animal Health, Hungarian University of Agriculture and Life Sciences, Guba Sándor u. 40, Kaposvár H-7400, Hungary.
Edward AgyarkoAgribiotechnology and Precision Breeding for Food Security National Laboratory, Institute of Physiology and Nutrition, Department of Physiology and Animal Health, Hungarian University of Agriculture and Life Sciences, Guba Sándor u. 40, Kaposvár H-7400, Hungary.
András SzabóAgribiotechnology and Precision Breeding for Food Security National Laboratory, Institute of Physiology and Nutrition, Department of Physiology and Animal Health, Hungarian University of Agriculture and Life Sciences, Guba Sándor u. 40, Kaposvár H-7400, Hungary.ORCID https://orcid.org/0000-0002-5315-0024
Miklós PoórDepartment of Laboratory Medicine, Medical School, University of Pécs, Ifjúság útja 13, Pécs H-7624, Hungary.ORCID https://orcid.org/0000-0003-1425-7459

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human serum albumin (HSA) maintains the oncotic pressure in the blood, also having buffer and antioxidant functions. Furthermore, numerous ligand molecules are circulating dominantly in albumin-bound form in the intravascular water space. The formation of stable ligand-albumin complexes commonly has significant physiological, pharmacological, and/or toxicological importance. Regarding ligand-HSA interactions, certain studies show controversial results that may have partly resulted from the differences between the protein preparations applied. To test this hypothesis, 10 HSA preparations were obtained, and then their albumin and free fatty acid content, fructosamine and free thiol levels, antioxidant capacity, fluorescence emission spectra, and ligand binding ability were examined. Our results demonstrate that sometimes even major differences can be observed when we compare these proteins. Therefore, the precise specification and the careful selection of HSA preparations seem to be reasonable.

Identifiers

PMID41078838
PMCPMC12509120

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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.