[Oxidative modification and change of intramolecular hydrophobicity of hemoglobin A during incubation of human erythrocytes in Fenton's medium].
It has been established by method of fluorescentive spectroscopy with using of zond FNA (N-phenilnaftilamine) that under incubation of human erythrocytes in Fenton's system (under intensive generation of oxygen active forms) the hydrophobicity of major hemoglobin fraction is lowered. The changes in the state of hemoglobin A intramolecular structure are correlated with formation of oxidative modification products. It has been shown that aldehydes and ketones of neutral character, which may be oxidative modification products of hydrophobic aminoacid residues, have the highest coefficient of correlation (r =-0.95).
Kazakova
V V
VV
Elkina
N M
NM
D018929:Cell Culture Techniques; D002478:Cells, Cultured; D016895:Culture Media, Serum-Free; D004912:Erythrocytes / Q000166:cytology* / Q000378:metabolism; D006441:Hemoglobin A / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D006861:Hydrogen Peroxide; D057927:Hydrophobic and Hydrophilic Interactions; D007501:Iron; D018384:Oxidative Stress; D017382:Reactive Oxygen Species / Q000378:metabolism*; D013997:Time Factors
D016895:Culture Media, Serum-Free; C045076:Fenton's reagent; D017382:Reactive Oxygen Species; D006441:Hemoglobin A; D006861:Hydrogen Peroxide; D007501:Iron