Radiation-induced changes of structural and functional properties of human hemoglobin
- 1 March 1989
- journal article
- research article
- Published by Springer Nature in Radiation and Environmental Biophysics
- Vol. 28 (1) , 47-58
- https://doi.org/10.1007/bf01209722
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.This publication has 20 references indexed in Scilit:
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