ArticlePloS one2020
Expression, purification and initial characterization of human serum albumin domain I and its cysteine 34.
Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.
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Who cites it
8 citing papers in PubMed, 1 synthesis or guideline pooled it, 12 citations in OpenAlex.
- The role of serum albumin and albumin-related nutritional indices in predicting post-stroke cognitive impairment: a systematic review and meta-analysis.Frontiers in neurology · 2025Pooled it
- Comparative Characterisation of Five Plasma-Derived Human Serum Albumin Preparations: Structural Integrity, Functional Properties, and Quality Attributes.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Formation of the intradimer disulfide bond in human calprotectin maintains metal-withholding function and tunes proteolytic susceptibility.Chemical science · 2026Article
- A simple and effective method to remove pigments from heterologous secretory proteins expressed in Pichia pastoris.Advanced biotechnology · 2024Article
- Albumin Thiolation and Oxidative Stress Status in Patients with Aortic Valve Stenosis.Biomolecules · 2023Article
- Graphene Oxide-Protein-Based Scaffolds for Tissue Engineering: Recent Advances and Applications.Polymers · 2022Review
- Structural and Biochemical Features of Human Serum Albumin Essential for Eukaryotic Cell Culture.International journal of molecular sciences · 2021Review
- Biomonitoring of Ambient Outdoor Air Pollutant Exposure in Humans Using Targeted Serum Albumin Adductomics.Chemical research in toxicology · 2021Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human serum albumin presents in its primary structure only one free cysteine (Cys34) which constitutes the most abundant thiol of plasma. An antioxidant role can be attributed to this thiol, which is located in domain I of the protein. Herein we expressed domain I as a secretion protein using the yeast Pichia pastoris. In the initial step of ammonium sulfate precipitation, a brown pigment co-precipitated with domain I. Three chromatographic methods were evaluated, aiming to purify domain I from the pigment and other contaminants. Purification was achieved by cation exchange chromatography. The protein behaved as a non-covalent dimer. The primary sequence of domain I and the possibility of reducing Cys34 to the thiol state while avoiding the reduction of internal disulfides were confirmed by mass spectrometry. The reactivity of the thiol towards the disulfide 5,5´-dithiobis(2-nitrobenzoate) was studied and compared to that of full-length albumin. A ~24-fold increase in the rate constant was observed for domain I with respect to the entire protein. These results open the door to further characterization of the Cys34 thiol and its oxidized derivatives.
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Registered trials
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