Damage to hemoglobin by radiation-generated serum albumin radicals. |
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| Authors: | M Pucha?a Z Szweda-Lewandowska |
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| Institution: | 1. Department of Molecular Biophysics, University of Łódź, Banacha 12/16, 90-237 Łódź, Poland;1. Department of Anesthesiology, Cangzhou Central Hospital, Cangzhou, China;2. Department of Gerontology, Cangzhou Central Hospital, Cangzhou, China;1. Division of Anesthesiology and Pain Medicine, Children’s National Medical Center, The George Washington University School of Medicine and Health Sciences;2. Department of Anesthesiology, College of Physicians and Surgeons of Columbia University, 622W. 168th Street, New York, NY 10032, USA;1. Department of Pediatrics, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, OH 44106-4984, USA;2. Pediatric Respiratory Medicine, University of Virginia School of Medicine, Charlottesville, VA 22908, USA;3. Division of Pulmonary, Critical Care, and Sleep Medicine, University Hospital Case Medical Center and the Louis Stokes Cleveland DVA Medical Center, Case Western Reserve University, Cleveland, OH 44106, USA;1. Department of Chemicals and Radiation, Norwegian Institute of Public Health, Oslo 0403, Norway;2. Litron Laboratories, Rochester, NY 14623, United States |
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| Abstract: | We have studied the effects of the interaction of radiation generated human serum albumin radicals (HSA*) with human hemoglobin molecules (Hb). Diluted Hb aqueous solutions were irradiated under N2O or argon without HSA and in the presence of HSA. Analysis of Hb absorbance spectra in the visible range, cross-linking of HSA* radicals with Hb molecules and functional properties of Hb were investigated. The degree of Hb destruction estimated on the basis of changes in the absorption spectra indicated that the effectiveness of HSA* radicals generated under N2O for Hb destruction was approximately equal to that of *OH radicals. In this case mainly *OH radicals formed the secondary HSA* radicals. However, during the irradiation Hb + HSA under argon the presence of equivalent amounts of oxidizing and reducing products of water radiolysis lowers the degree of Hb destruction. Some reactions of HSA* radicals with Hb molecules lead to the formation of covalent bonds between the molecules of both proteins. The following types of hybrids could be distinguished: Hb monomer-HSA, Hb dimer-HSA and higher aggregates. Structural changes of Hb by HSA* radicals were reflected by alterations in the oxygen affinity (increase) and cooperativity (decrease) of Hb. The results obtained indicate that in the experimental systems studied, the HSA* radical reactions with Hb molecules are favoured over recombination reactions of HSA* radicals. On this basis one can suggest that in the studied systems Hb plays the role of an acceptor of radical energy located on HSA. |
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