Abstract
The effect of 0.1–10% nitrosohemoglobin (HbNO) on the functional properties of human oxyhemoglobin (HbO2) was studied before and after UV irradiation at 151–453 J/m2. Oxygen binding analysis showed that HbNO intensified the first stage of oxygenation and weakened the cooperative interactions in the tetramer, decreasing the affinity of hemoglobin for oxygen at physiologically important oxygen partial pressures (40–100 mm Hg). Mixtures of HbO2 and HbNO were highly resistant to “therapeutic” doses of UV irradiation. Since the functional activity of hemoglobin depended nonlinearly on the concentration of HbNO in the mixture, it was assumed that sophisticated interactions of HbO2 and HbNO yielded a new product differing in properties from the initial components.
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