[Structure-activity changes in human hemoglobin induced by UV-light and serotonin]

Basic indices of oxygen-binding properties of the human hemoglobin solutions modified by the UV-light (240-390 nm) in dose range 151-604 J/m2 together with serotonin (10(-5)-10(-3) mol/l) have been analysed by means of spectrophotometry registration of the oxyhemoglobin dissociation curves. In these conditions biogenic amine displays maximum photoprotective effect at the concentration 4 x 10(-4) mol/l. At the highest concentrations serotonin exert photosensibilitive that influences the course of the protein molecule disorganisation. It has been demonstrated that three-dimensional surfaces analysis can be used to forecast the influence of the serotonin photoprotection on the hemoglobin functional activity.