[Study of soluble proteins of mouse crystalline lenses (normal and in cataract)].

The water-soluble proteins from mice lenses (normal and cataract lenses) were investigated by methods of absorption spectrophotometry and kinetics of UV-induced radical decay. General characteristic of internal structure of extraction proteins was investigated by recombination kinetic method. It was shown that concentration of water-soluble proteins lowered ten times in lenses of mature cataract, i.

[The effect of the charge of aromatic amino acid, peptide and protein molecules on the rate of radical formation during UV-irradiation].

It has been shown that the rate of radical formation under UV-irradiation of some aromatic amino acids, peptides and proteins abruptly increases with pH rise in the region 9.5-11. This effect is observed only in the case when the total charge of the molecule after ionization remains negative.

[Accumulation of UV-induced radicals in proteins with various degree of aggregation].

Accumulation of radicals UV-induced in protein solutions at 77 K was investigated. It has been found that in each molecule of small proteins true solutions only one ionization proceeds and two radicals are formed. The limiting number of radicals per one protein molecule decreases with the increase of their aggregation level.