Study of the state of hemoglobin in human erythrocytes in the conditions of oxidative stress of various intensity
Keywords:
membrane-bound hemoglobin; oxyhemoglobin; methemoglobin; hemichrome; hemoglobin absorption spectra; Sore bandAbstract
Oxidative stress was created by introducing hydrogen peroxide (concentration range 10-6 ‑ 0.1 M) into the erythrocyte incubation medium. The different concentrations effect of hydrogen peroxide to the content of membrane-bound hemoglobin, ligand forms of the cytoplasmic fraction hemoglobin and the composition of membrane-bound hemoglobin were studied by spectrophotometry and subsequent analysis of hemoglobin absorption spectra in the range of 350 - 650 nm. Quantitative changes of intracellular and extracellular hydrogen peroxide were tested. It is shown that hydrogen peroxide in the concentration range 5×10-3 to 0.1 M has a negative effect on the cell surface state, causing the rearrangement of the lipid bilayer. These processes result in the conversion of oxyhemoglobin to hemichrome and its irreversible binding to membrane lipids.
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