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Dokl Biochem Biophys. 2017 May;474(1):231-235. doi: 10.1134/S1607672917030218. Epub 2017 Jul 20.

Modification of human serum albumin under induced oxidation.

Author information

1
Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 119334, Russia. maria.g.gorobets@gmail.com.
2
Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 119334, Russia.
3
Moscow Institute of Physics and Technology, Dolgoprudny, Moscow oblast, Russia.
4
Institute for Energy Problems of Chemical Physics, Russian Academy of Sciences, Moscow, Russia.
5
Skolkovo Institute of Science and Technology, Skolkovo, 143025, Russia.

Abstract

For the first time, by using the complex of physicochemical methods (mass-spectrometry, differential scanning calorimetry, spectrofluorimetry, method of spectral and fluorescent probes, dynamic light scattering, and UV spectrophotometry), the oxidation-mediated modification of chemical and spatial structure of albumin has been studied. All albumin structural regions are subjected to oxidation, methionine and aromatic amino acids primarily involved in oxidation. The albumin melting shows a decrease in thermal stabilization of the structure and changing of aggregation upon oxidation. The change in physical and chemical properties of albumin under different quantity of the oxidizer has been analyzed.

PMID:
28726091
DOI:
10.1134/S1607672917030218
[Indexed for MEDLINE]

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