[Modifying effect of alcohols on the radiation transformations of serum albumin]. / O modifitsiruiushchem vliianii spirtov na radiatsionnye prevrashcheniia syvorotochnogo al'bumina.

The method of roentgenochemoluminescence was used to study the reactions of alcohol radicals with tryptophanyl residues of protein. These radicals exhibited a high reactivity. In a series of alcohol radicals and 3-oxy-pyridine derivatives, a positive correlation was revealed between the rate of the reaction of radicals with the macromolecule and the hydrophobic character of free radicals.

[Influence of superoxide dismutase on photo- and x-ray chemoluminescence of serum albumin and glycyltryptophan solutions]. / Vliianie superoksiddismutazy na foto- i rentgenokhemiliuminestsentsiiu rastvorov glitsiltriptofana i syvorotochnogo al'bumina.

Enzyme superoxide dismutase is shown to decrease photo- and X-ray chemoluminescence when added both before and after irradiation. The relationship was established between chemoluminescence yield and the enzyme concentration. Chemoluminescence is supposed to be initiated by the reaction of free radicals of the peptide (protein) with superoxide anion-radicals: O2-.

[Comparative study of the radiation oxidation and x-ray chemiluminescence of globular proteins]. / Sravnitel'noe issledovanie radiatsionnogo okisleniia i rentgenokhemiliuminestsentsii nekotorykh globuliarynkh belkov.

Regularities of radiation oxidation (oxygen absorption for irradiation) and X-ray chemoluminescence of human serum albumin solutions have been studied. The oxidative rate was shown to be proportional to chemoluminescence intensity under various experimental conditions. the yield values for radiation oxidation of natural amino acids, glycyl-tryptophane and some other proteins were obtained. These values for amino acids changed in the range of 1.4 to 6, the mean value for amino acid yield was about 3.5 oxygen molecules/100 eV. Protein oxidation yield was in the range of 1.6 to 4. Correlation of the yields with respect to macromolecule spiralization was carried out. The difference in the yields of radiation oxidation protein can be related to higher duration of free radical life-span of amino acid residues forming the spirals that promotes formation of peroxy radicals. The difference of chemoluminescence yields for various proteins can be accounted for by different locations of tryptophan residues accessible for active products of water radiolysis and by the presence of various quantities of arginine in macromolecules. The mechanisms of chemical conversions of tryptophanyl peroxy radicals resulting in the formation of electron-excited states were discussed.