[Features of photochemical properties of hemoglobin under native conditions]

The photochemistry of human hemoglobin (Hb) in the blood and blood serum (lambda = 254-578 nm) was studied, using spectrophotometric methods. The Hb photochemistry is a complex set of photoreactions leading to successive photoconversions of Hb forms: from oxy- to met- to deoxy- and, finally, to carboxy-form. The photodestruction of Hb and the photoreactions involving other serum proteins were found to occur simultaneously. In the blood Hb photomodifications are localized directly in erythrocytes. The conditions necessary for the photo--induced rupture of erythrocyte membranes and the subsequent release of Hb into the blood plasma, were determined. Although the general characteristics of Hb photochemistry are the same for model systems and for native conditions, there are some distinctions in the effectiveness of the photoconversion. It seems likely that the observed effects are due to the antioxidant properties of the serum. These properties may be the cause of the inhibition of blood photohemolysis upon irradiation (lambda greater than or equal to 300 nm).