<p>The protective effect of sodium selenite (Na<sub>2</sub>SeO<sub>3</sub>) on the oxidative degradation of hemoglobin induced by hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>) was studied by recording the resulting two fluorescent products of heme breakdown (λ<sub>excitation</sub> = 321 nm, λ<sub>emission</sub> = 460 nm) and (λ<sub>excitation</sub> = 465 nm, λ<sub>emission</sub> = 525 nm). It has been established that sodium selenite (Na<sub>2</sub>SeO<sub>3</sub>) inhibits the development of oxidative modification of hemoglobin (depletion of HbO<sub>2</sub> and accumulation of MetHb and FerrylHb), which is reflected in a noticeable 20–30% decrease in fluorescence peaks, reflecting the oxidative destruction of heme in the absence of the contribution of antiperoxide enzymes (CAT, GPX, and PRDX-2) in H<sub>2</sub>O<sub>2</sub> utilization. This raises the question of the independent AO significance of selenium in hemoglobin, in its protection from peroxide effects without the GPX mechanism of Н<sub>2</sub>О<sub>2</sub> utilization.</p>

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Selenium as a Protector against Hydrogen Peroxide Oxidative Degradation of the Heme of Hemoglobin without the Glutathione Peroxidase Mechanism

  • T. M. Huseynov,
  • S. M. Rahmanova,
  • F. R. Mehraliyeva

摘要

The protective effect of sodium selenite (Na2SeO3) on the oxidative degradation of hemoglobin induced by hydrogen peroxide (H2O2) was studied by recording the resulting two fluorescent products of heme breakdown (λexcitation = 321 nm, λemission = 460 nm) and (λexcitation = 465 nm, λemission = 525 nm). It has been established that sodium selenite (Na2SeO3) inhibits the development of oxidative modification of hemoglobin (depletion of HbO2 and accumulation of MetHb and FerrylHb), which is reflected in a noticeable 20–30% decrease in fluorescence peaks, reflecting the oxidative destruction of heme in the absence of the contribution of antiperoxide enzymes (CAT, GPX, and PRDX-2) in H2O2 utilization. This raises the question of the independent AO significance of selenium in hemoglobin, in its protection from peroxide effects without the GPX mechanism of Н2О2 utilization.