On the hydrodynamics and temperature dependence of the solution conformation of human serum albumin from viscometry approach.

The paper presents the results of viscosity determinations on aqueous solutions of human serum albumin (HSA) at a wide range of concentrations and at temperatures ranging from 5 to 45 degrees C. On the basis of a modified Arrhenius formula and Mooney's equation, the viscosity-temperature and viscosity-concentration dependence of the solutions are discussed. The effective specific volume, the activation energy and entropy of viscous flow for hydrated HSA were calculated. Different models of HSA molecule are discussed and the best one-from the hydrodynamic point of view-was established. At low concentration limit, such rheological quantities as the intrinsic viscosity and Huggins coefficient were obtained. Using the dimensionless parameter [eta]c, the existence of three characteristic ranges of concentrations: diluted, semi-diluted and concentrated, was shown.