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Abstract
The influence of electromagnetic field in wide range of frequency (extra low frequency magnetic field, monochromatic laser light 840 nm, ultraviolet light) and static magnetic field on the stability of aqueous and NaCl 0.9% haemoglobin solutions was studied using differential scanning calorimetry (DSC) method. Three steps of denaturation process can be derived from experimental data. The shifts of transition temperatures are more marked for NaCl 0.9% than for aqueous solutions. The results suggest that static magnetic field is effective in protecting protein, while ultraviolet radiation destabilises haemoglobin. The laser light and alternating magnetic field have a little effect on the thermal stability of haemoglobin.
Nagy E., Jeney V., Yachie, A. és mtsai: Oxidation of hemoglobin by lipid hydroperoxide associated with low-density lipoprotein (LDL) and increased cytotoxic effect by LDL oxidation in heme oxygenase-1 (HO-1) deficiency. Cell Mol. Biol., 2005, 51
Abstract
Structural modifications of human adult oxyhemoglobin in concentrated solution were studied by Mössbauer and positron life-time spectroscopies. The effects of non-sterile degradation and irradiation by 
-rays were compared by both techniques. It was found that positron annihilation parameters were sensitive to the structural modifications of hemoglobin molecules in solution and could be related with the conformational states of hemoglobin.
