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Updated: May 20, 2026

Assessment of Cellular Oxidation using a Subcellular Compartment-Specific Redox-Sensitive Green Fluorescent Protein
Published on: June 18, 2020
Studies of oxidant-induced changes in albumin transport function with a fluorescent probe k-35. Effect of
O A Azizova1, A V Aseychev, E M Beckman
1Laboratory for Biophysical Bases of Pathology, Laboratory for Biophysical Methods of Diagnostics, Federal State Institution, Institute of Physicochemical Medicine, Federal Medical-Biological Agency, Moscow, Russia.
Abstract:
The dynamics of changes in albumin transport function during hypochlorite-induced oxidation of isolated albumin in blood plasma and serum was studied with a fluorescent probe K-35. Binding of the probe K-35 to albumin was characterized by effective concentration of albumin. Oxidative modification of proteins was evaluated by the content of carbonyl products of protein oxidation and bityrosine fluorescent products. Oxidation with hypochlorite was accompanied by a decrease in the effective concentration of albumin in albumin, diluted plasma, and serum and accumulation of carbonyl products of protein oxidation and bityrosine fluorescent products. The decrease in the effective concentration of albumin during oxidation with hypochlorite can be explained by oxidative damage to albumin binding sites. Oxidative modification of probe K-35 binding sites with hypochlorite contributes to a decrease in effective concentration of albumin under pathological conditions.
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