title: The influence of ferrylhemoglobin and methemoglobin on the human erythrocyte membrane.
abstract: The aim of the study was to examine and compare the effects of methemoglobin (metHb) and ferrylhemoglobin (ferrylHb) on the erythrocyte membrane. Kinetic studies of the decay of ferrylhemoglobin (*HbFe(IV)=O denotes ferryl derivative of hemoglobin present 5 min after initiation of the reaction of metHb with H(2)O(2); ferrylHb) showed that autoredecay of this derivative is slower than its decay in the presence of whole erythrocytes and erythrocyte membranes. It provides evidence for interactions between ferrylHb and the erythrocyte membrane. Both hemoglobin derivatives induced small changes in the structure and function of the erythrocyte membrane which were more pronounced for ferrylHb. The amount of ferrylHb bound to erythrocyte membranes increased with incubation time and, after 2 h, was twice that of membrane-bound metHb. The incubation of erythrocytes with metHb or ferrylHb did not influence osmotic fragility and did not initiate peroxidation of membrane lipids in whole erythrocytes as well as in isolated erythrocyte membranes. Membrane acetylcholinesterase activity increased by about 10% after treatment of whole erythrocytes with both metHb and ferrylHb. ESR spectra of membrane-bound maleimide spin label demonstrated minor changes in the conformation of label-binding proteins in ferrylHb-treated erythrocyte membranes. The fluidity of the membrane surface layer decreased slightly after incubation of erythrocytes and isolated erythrocyte membranes with ferrylHb and metHb. In whole erythrocytes, these changes were not stable and disappeared during longer incubation.
authors.affiliation: Department of Molecular Biophysics, University of Lodz, Lodz, Poland.
authors.forename: Malgorzata
authors.initials: M
authors.lastname: Sztiller
authors.forename: Mieczyslaw
authors.initials: M
authors.lastname: Puchala
authors.forename: Aleksandra
authors.initials: A
authors.lastname: Kowalczyk
authors.forename: Grzegorz
authors.initials: G
authors.lastname: Bartosz
mesh_terms: D000110:Acetylcholinesterase / Q000378:metabolism; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006454:Hemoglobins / Q000737:chemistry*; D006801:Humans; D007501:Iron / Q000737:chemistry; D015227:Lipid Peroxidation; D008055:Lipids / Q000737:chemistry; D008706:Methemoglobin / Q000737:chemistry*; D016877:Oxidants / Q000737:chemistry; D011487:Protein Conformation; D013053:Spectrophotometry; D013113:Spin Labels; D013997:Time Factors
chemical_list: D006454:Hemoglobins; D008055:Lipids; D016877:Oxidants; D013113:Spin Labels; C517773:ferrylhemoglobin; D008706:Methemoglobin; D007501:Iron; D000110:Acetylcholinesterase