Radiation-induced changes of structural and functional properties of human hemoglobin. II. Structural and functional characterization of irradiated deoxyhemoglobin.
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.
Szweda-Lewandowska
Z
Z
Chair of Biophysics, University of Lódz, Poland.
Puchała
M
M
Osmulski
P A
PA
Rosin
J
J
D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006454:Hemoglobins / Q000032:analysis / Q000528:radiation effects*; D006801:Humans; D010100:Oxygen / Q000378:metabolism; D011108:Polymers; D013053:Spectrophotometry
D006454:Hemoglobins; D011108:Polymers; C100003:deoxyhemoglobin; D010100:Oxygen