Macromolecular sizes of serum albumins in its aqueous solutions

Abstract

Changes in the structure and sizes of human and bovine serum albumins as well as polyvinyl alcohol macromolecules in aqueous solutions depending on temperature, concentration, and acid-base balance (pH) of the solutions are discussed. It is taken into consideration that the change in the hydrodynamic radius of a macromolecule is one of the indicators of structural phase transformations of globular proteins. The methods of the macromolecular radii determination from the shear viscosity and the self-diffusion of macromolecules in solutions are discussed. The hydrodynamic radius values of albumin and polyvinyl alcohol macromolecules obtained by the above methods are thoroughly compared. Consideration of these questions provides us with important information on the nature of the binding of water molecules with protein macromolecules.