[Structural transitions of serum proteins in solutions during high- and low-temperature dehydration].
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.
Darman'ian
E B
EB
D000596:Amino Acids / Q000737:chemistry; D003890:Desiccation; D004578:Electron Spin Resonance Spectroscopy; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013055:Spectrophotometry, Infrared; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature
D000596:Amino Acids; D012710:Serum Albumin, Bovine
Strukturnye prevrashcheniia syvorotochnogo belka v rastvorakh pri vysoko- i nizkotemperaturnom obezvozhivanii.