Structural transitions of serum proteins in solutions during high- and low-temperature dehydration
Darman'ian, E.B.
Prikladnaia Biokhimiia i Mikrobiologiia 33(2): 183-188
1997
ISSN/ISBN: 0555-1099 PMID: 9157416 Document Number: 472969
Infrared and ultraviolet spectroscopy, potentiometric titration, and refractometry, as well as analysis of lysine, tryptophan, and tyrosine availability, and enzymic hydrolysis were used to establish that high-temperature and low-temperature dehydration of solutions of serum protein is accompanied by a rearrangement of its molecular structure, resulting in changes in the number of polar radicals and hydrophobic bonds, intermolecular and intramolecular interactions, and the formation of a new stable conformation. Comparison of the two methods of dehydration showed that cryoconcentration resulted in a greater accessibility of the protein molecule to chemical agents and proteolytic enzymes, whereas heating had an opposite effect.