Abstract
The paper presents the results of the study of molecular light scattering (MLS) by aqueous solutions of human serum albumin.Using static light scattering methods, it was found that the concentration dependence of molecular scattering intensity differs from similar dependences for solutions of polymers such as polyethylene glycol or polyvinyl alcohol.In contrast, the concentration dependences of MLS intensity have a scattering peak at concentrations of 6%, which can be considered as anomalous scattering similar to the scattering of light in aqueous solutions of some substances, more often - alcohols.The position of the light scattering peak obtained in the work coincides with the characteristic point of aqueous solutions of albumins of various origins, which is determined by the concentration of the protein component in the blood plasma of mammals.A detailed analysis of the obtained results requires new studies on the temperature dependence of the MLS intensity peaks and the results of laser correlation spectroscopy of the intensity of scattered light.
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