REVIEW

Serum albumin as a source of and a target for free radicals in pathology

Sozarukova MM, Proskurnina EV, Vladimirov YuA
About authors

Department of Medical Biophysics, Faculty of Fundamental Medicine,
Lomonosov Moscow State University, Moscow, Russia

Correspondence should be addressed: Madina Sozarukova
Lomonosovsky prospekt, d. 31, corp. 5, Moscow, Russia, 117192; moc.liamg@usmavokurazos

About paper

Funding: this study was supported by the Russian Science Foundation (project no. 14-15-00375).

Received: 2015-09-30 Accepted: 2015-12-09 Published online: 2017-01-05
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Fig. 1. Location of fatty acid- and Cu-binding sites; location of probes I and II in domains I, II and III in HSA structure
Fig. 2. Fluorescence spectra obtained in the experiments. (1) HSA (0.66 μm) and AAPH (2.5 mM), figures next to curves show incubation time. (2) HSA (0.6 μm), Н2О2 (3 mM) and Со2+ (0.3 mM), figures next to HSA + Н2O2 + Со2+ curves show time after introducing Со2+ to the system: 0, 3, 6, 9 and 15 minutes. (3) HSA (0.6 μm), figures next to curves show UV-irradiation dosage, kJ/cm2. (4) HSA (fraction isolated from blood plasma and diluted 1:100) combined with neutrophils stimulated by barium sulfate and FMLP
Fig. 3. Changes in fluorescent and antioxidant properties of HSA exposed to different doses of UV-irradiation. (1) HSA fluorescence spectra (0.66 μm); the protein was exposed to different doses of UV-irradiation (figures show the dosage, J/cm2: 0 — native protein, 1 — 0.050, 2 — 0.200, 3 — 0.400, 4 — 0.600, 5 — 0.800, 6 — 1.000). (2) Chemiluminescence curves of HSA (0.66 μm) exposed to different doses of UV-irradiation (figures next to curves show the dosage, J/cm2) in the system containing phosphate buffer solution (PB) (37 °С), AAPH (2.5 mM), luminol (Lum) (2 μm), system total volume 1.000 ml
Fig. 4. Comparison of HSA fluorescence changes (0.66 μm) (λ340 max = 337 nm) and the increase in the total antioxidant activity (tlat, min) with the increased dosage of short wavelength radiation, J/cm2