[Tryptophan fluorescence of erythrocyte ghosts following irradiation and Fe2+ initiation of lipid peroxidation].
It was shown that under the effect of Fe2+-initiated lipid peroxidation and ionizing radiation tryptophan fluorescence parameters (i.e. intensity and polarization) were subjected to similar changes. Shortly (15 min) after irradiation no changes were observed in the level of products reacting with thiobarbituric acid. It is concluded that the process and products of lipid peroxidation do not markedly contribute to the postirradiation alteration of tryptophan fluorescence. At the same time additional postirradiation damages to proteins can be attributed to activation of lipid peroxidation.
D000818:Animals; D003037:Cobalt Radioisotopes; D004910:Erythrocyte Membrane / Q000528:radiation effects*; D005720:Gamma Rays; D066298:In Vitro Techniques; D007501:Iron / Q000494:pharmacology*; D008054:Lipid Peroxides / Q000097:blood*; D051381:Rats; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000097:blood*
D003037:Cobalt Radioisotopes; D008054:Lipid Peroxides; D014364:Tryptophan; D007501:Iron
Issledovanie triptofanovoĭ fluorestsentsii teneĭ éritrotsitov posle oblucheniia i initsiatsii perekisnogo okisleniia lipidov Fe2+.