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.
Original language | English (US) |
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Pages (from-to) | 47-58 |
Number of pages | 12 |
Journal | Radiation and Environmental Biophysics |
Volume | 28 |
Issue number | 1 |
DOIs | |
State | Published - Mar 1989 |
Externally published | Yes |
ASJC Scopus subject areas
- General Environmental Science
- Radiation
- Biophysics