The influence of metmyoglobin and ferrylmyoglobin on the human erythrocyte membrane.
Preliminary experiments revealed that ferrylmyoglobin decayed more slowly in the absence than in the presence of intact erythrocytes and erythrocyte membranes. This suggested the existence of interactions between FerrylMb and the erythrocyte membrane. Subsequent studies examined the influence of FerrylMb on the membrane of intact erythrocytes and on isolated erythrocyte membranes. The incubation of intact erythrocytes with FerrylMb did not influence their osmotic fragility or the fluidity of their membranes; the level of peroxidation of the membrane lipids increased only slightly (there was only a slight increase in the level of membrane lipid peroxidation). The activity of acetylcholinesterase significantly increased after 15 minutes of incubation, whereas longer incubation did not lead to any changes in the activity of this enzyme. The incubation of isolated erythrocyte membranes with FerrylMb resulted in an increase in their fluidity and a significant rise in the level of lipid peroxidation.
Sztiller
Małgorzata
M
University of Łódź, Department of Molecular Biophysics, Banacha 12/16, Łódź, Poland.
Puchała
Mieczysław
M
D000110:Acetylcholinesterase / Q000378:metabolism; D016880:Anisotropy; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism*; D004912:Erythrocytes / Q000187:drug effects / Q000378:metabolism*; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology; D008786:Metmyoglobin / Q000187:drug effects / Q000378:metabolism*; D016877:Oxidants / Q000494:pharmacology; D013053:Spectrophotometry
D016877:Oxidants; C028048:ferrylmyoglobin; D008786:Metmyoglobin; D006861:Hydrogen Peroxide; D000110:Acetylcholinesterase