Abstract
A relation between the water properties and the behavior of aqueous solutions of albumin, the main protein component of human blood plasma, has been analyzed. The dependence of the pH index of acid-base balance in aqueous albumin solutions on the albumin concentration is experimentally studied. It is shown that the temperature dependences of pH in biological solutions are determined by the properties of water, and the concentration ones by the concentration of a protein component. It is albumin that makes the main contribution to the pHs of blood and blood plasma, and it should be considered as a factor that maintains the equilibrium pH value. It is shown that the most characteristic changes in the concentration dependences of the density and shear viscosity of human plasma occur at a protein concentration corresponding to the percolation threshold. A characteristic dimerization of albumin macromolecules is assumed to take place at the percolation threshold, which corresponds to the superposition on one another of heart-shaped medallions representing the spatial forms of albumin. The dependences of the effective radii of polyvinyl alcohol and albumin macromolecules on the solution temperature and concentration are demonstrated to be an indicator that water plays a decisive role in the formation of basic properties of biosolutions. In particular, it is responsible for the presence of an upper temperature limit of 42 ∘C for the existence of living matter. The universal nature of the water influence manifests itself in that the water properties affect the behavior of both the classic PVA polymer and protein biomolecules.
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