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. 1989;28(1):47-58.
doi: 10.1007/BF01209722.

Radiation-induced changes of structural and functional properties of human hemoglobin. II. Structural and functional characterization of irradiated deoxyhemoglobin

Z Szweda-Lewandowska  1 , M Puchała, P A Osmulski, J Rosin
Affiliations

Radiation-induced changes of structural and functional properties of human hemoglobin. II. Structural and functional characterization of irradiated deoxyhemoglobin

Z Szweda-Lewandowska et al. Radiat Environ Biophys. 1989.

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.

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