M G Gorobets, L A Wasserman, A D Vasilyeva, A V Bychkova, P G Pronkin, A E Bugrova, M I Indeykina, N G Shilkina, M L Konstantinova, A S Kononikhin, E N Nikolaev, M A Rosenfeld
Doklady. Biochemistry and biophysics 2017 MayFor 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.
M G Gorobets, L A Wasserman, A D Vasilyeva, A V Bychkova, P G Pronkin, A E Bugrova, M I Indeykina, N G Shilkina, M L Konstantinova, A S Kononikhin, E N Nikolaev, M A Rosenfeld. Modification of human serum albumin under induced oxidation. Doklady. Biochemistry and biophysics. 2017 May;474(1):231-235
PMID: 28726091
View Full Text