Abstract
The freezing and thawing of specific antitoxic serum proteins without a cryoprotective agent results in a reduction of titer. A freezing regimen has been chosen and the cryoprotectant PEO-400 has been added to prevent a reduction in activity of antitetanus serum after 6 months of storage in liquid nitrogen. The study of dielectric properties of proteins in solution and measurements of spin-label rotational diffusion have made it possible to estimate the degree of dehydration of protein molecules in the presence of PE-400. We suggest that a damping coat of PEO forms around protein molecules at the expense of hydrophilic and hydrophobic interactions. We further suggest that this damping coat is one of the main mechanisms of cryoprotective action of polyethylene oxide, and possibly of other cryoprotectants such as glycerol.
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