title: Radiation-induced changes of structural and functional properties of human hemoglobin. II. Structural and functional characterization of irradiated deoxyhemoglobin.
abstract: Gel filtration and SDS-PAGE separation of hemoglobin (Hb) irradiated under argon or N2O show formation of covalent-aggregated Hb molecules. The production of covalent bonds is attributed mainly to the action of hydroxyl radicals, because addition of ethanol, a scavenger of these radicals, suppresses this reaction to a great extent. The oxidized heme iron forming metHb or hemichromes is found in all the separated fractions of irradiated Hb. It is also found that the radiation-modified Hb molecules exhibit a decrease of co-operative binding of oxygen.
authors.affiliation: Chair of Biophysics, University of Lódz, Poland.
authors.forename: Z
authors.initials: Z
authors.lastname: Szweda-Lewandowska
authors.forename: M
authors.initials: M
authors.lastname: Puchała
authors.forename: P A
authors.initials: PA
authors.lastname: Osmulski
authors.forename: J
authors.initials: J
authors.lastname: Rosin
mesh_terms: D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006454:Hemoglobins / Q000032:analysis / Q000528:radiation effects*; D006801:Humans; D010100:Oxygen / Q000378:metabolism; D011108:Polymers; D013053:Spectrophotometry
chemical_list: D006454:Hemoglobins; D011108:Polymers; C100003:deoxyhemoglobin; D010100:Oxygen