Anesthetics expand partial molal volume of lipid-free protein dissolved in water: electrostriction hypothesis.

The present study was undertaken to critically examine whether the dilating action of inhalation anesthetics is specific to lipid membranes. Delipidated crystalline bovine serum albumin was used as a model and the density of a salt-free aqueous solution was measured by a high-precision oscillation densimeter. The partial molal volumes of albumin at infinite dilution were 50,326, 51,019 and 51,698 cm3 . mol-1, respectively at 293, 308 and 323 degrees K. From the difference between the present value and the volume of dry albumin, the number of electrostricted water molecules at the surface of albumin in aqueous solution at 293.15 degrees K is estimated to be about 720. Addition of diethylether to the albumin solution increased the partial molal volume of albumin, dose-dependently. At 57.88 mmolal, diethylether expanded the partial molal volume of albumin at 293 degrees K by 295 cm3 . mol-1 or 0.59%. This volume expansion does not include the space occupied by the anesthetic molecules in albumin. If the expansion can be assumed to be caused mainly by melting of electrostricted water molecules, about 110 water molecules were released from the protein surface. The partial molal volume of diethylether was increased when bound to albumin. The increase indicates that the contact between diethylether and water is partially destroyed and that high pressure squeezes out anesthetic molecules from the protein.