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The Effect of Gas-Discharge Plasma Radiation on Erythrocyte Protein Modification

The Effect of Gas-Discharge Plasma Radiation on Erythrocyte Protein Modification

Trofimova S.V., Burkhina О.Е., Piskaryov I.M., Ichetkina А.А., Solovyova Т.I., Astafieva К.А., Pugina Е.S., Ivanova I.P.
Key words: gas-discharge plasma radiation; protein modification; bityrosine and tryptophan fluorescence; UV-spectrum of proteins; erythrocyte protein fluorescence.
2014, volume 6, issue 3, page 14.

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The aim of the investigation was to estimate the effect of spark plasma radiation on oxidative protein modification in solutions and erythrocytes in experiments and in vitro.

Materials and Methods. Pulse spark discharge generating low-temperature plasma radiation was formed using an experimental device PILIMIN series IR-10 (Russia). The characteristics of a discharge were the following: capacity of pulse capacitor — 3.3 nF, ballast resistance — 10 MΩ, power supply voltage — 11 kV, pulse recurrence frequency — 10 Hz. Tryptophan, albumin, hemoglobin solutions, and erythrocyte suspensions of intact animals and animals with experimental sarcoma were used as research subjects. 4 ml samples were treated in sterile Petri plates. Structural state of tryptophan, albumin and hemoglobin molecules was assessed by UV absorption spectra. Oxidative protein damage degree in solutions and cells was estimated by bityrosine and tryptophan fluorescence.

Results. The increase of oxidative protein modification in solutions after spark discharge plasma radiation is due to the presence of complexes of tryptophan, albumin and hemoglobin molecules with nitro compounds, nitric radicals, hydroperoxyl radicals formed under discharge generation. Erythrocyte protein structures of animals with experimental sarcoma are characterized by more intense oxidative modification compared to erythrocytes of intact animals. Oxidative modification of erythrocyte proteins under plasma radiation to greater degree is due to the accumulation of bityrosine cross-links.


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