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

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

Research output: Contribution to journalArticle

7 Scopus citations

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 languageEnglish (US)
Pages (from-to)47-58
Number of pages12
JournalRadiation and Environmental Biophysics
Volume28
Issue number1
DOIs
StatePublished - Mar 1 1989
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Radiation
  • Environmental Science(all)

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