Electrocatalytic artificial carbonylation assay for observation of human serum albumin inter-individual properties
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
29723520
DOI
10.1016/j.ab.2018.04.025
PII: S0003-2697(18)30137-4
Knihovny.cz E-resources
- Keywords
- Binding capacity, Carbonylation, Electrocatalytic assay, Inter-individual variation, Protein oxidation, Serum albumin,
- MeSH
- Adult MeSH
- Electrochemical Techniques methods MeSH
- Protein Carbonylation * MeSH
- Humans MeSH
- Serum Albumin, Human metabolism MeSH
- Check Tag
- Adult MeSH
- Humans MeSH
- Male MeSH
- Female MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Serum Albumin, Human MeSH
Human serum albumin (HSA) is a multifunctional protein with ligand binding, transporting and buffering properties. Posttranslational modifications and ligand binding processes are closely related to albumin final functional status. In the last few decades, HSA has been characterized using a broad spectrum of methods, but quantitative data on the HSA's modifications among individuals have not been reported. The investigations presented here are based on the non-denaturing electrocatalytic screening of HSA samples isolated from the blood serum of healthy subjects. The electrocatalytic responses of the native protein (Rnat) varied depending on its modifications among individuals, which enable us to express the inter-individual variability. Consequently, the native HSA samples were subjected to ex vivo carbonylation with 50 mM methylglyoxal for 36 h. The differences between Rnat and the responses of artificially carbonylated protein (Rmod) corresponded with inter-individual binding capacity variations (ΔR = Rnat-Rmod). The coefficients of variation for the Rnat and ΔR values of purified HSA samples were estimated to be 8.5 and 23.2%, respectively. A sensitive non-denaturing electrocatalytic assay was utilized to provide new data about albumin inter-individual variations and evaluate its oxidative modifications and binding capacity, which could be used for further studies targeting not only on HSA but also other clinically important proteins.
Department of Clinical Biochemistry University Hospital Olomouc 1 P Pavlova 6 Olomouc Czech Republic
Department of Transfusion Medicine University Hospital Olomouc 1 P Pavlova 6 Olomouc Czech Republic
References provided by Crossref.org
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