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E E Fesenko

Publications and source records attributed to E E Fesenko.

130 records · Page 8Linked to original sources

[Molecular mechanisms of biological action of low magnetic fields. IV. Proteolysis of protein-DNAse 1 inhibitor in water phase under combined action of low constant and alternating magnetic fields adjusted to cyclotron resonance of polar amino acid ions].

It was shown that combined action of weak magnetic fields adjusted to cyclotronic frequencies of polar amino acids ions, on aqueous solutions of acidic non-histone protein-inhibitor of DNAase 1 led to proteolysis of this inhibitor. The fragments obtained as a result of proteolysis differ from the whole molecule by amino acid composition and the time of elution from column in case of HPLC.

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[Modulated extremely high frequency electromagnetic radiation of low intensity activates or inhibits respiratory burst in neutrophils depending on modulation frequency].

The influence of low-intensity modulated electromagnetic radiation of extremely high frequencies (EHF EMR) on synergistic reaction of calcium ionophore A23187 and phorbol ester PMA in activation of the respiratory burst of the peritoneal neutrophils of mice line NMRI was investigated. The production of reactive oxygen species by the neutrophils was estimated by luminol-dependent chemiluminescence technique. The cells were irradiated in the far field zone of the channel radiator for 20 min in the presence of A23187 and then were activated by PMA after switching off the irradiation. It was shown, that continuous EHF EMR (50 microW/cm2) inhibited quasi-resonantly the synergistic reaction. The maximum effect was about 25% at carrier frequency of 41.95 GHz. Modulated radiation with carrier frequency of 41.95 GHz and modulation frequency of 1 Hz activated the synergistic reaction, but at modulation frequencies of 0.1, 16 and 50 Hz inhibited one. At fixed modulation frequency of 1 Hz the nonlinear dependence of the effect on the carrier frequency was found. The synergistic reaction was activated in the frequency range of 41.95-42.05 GHz and was inhibited at the frequencies of 41.8-41.9 GHz. The effect was observed only at raised intracellular free calcium concentration and at calcium fluxes through plasma membrane. The obtained results prove the possibility of control over cell functioning by low-intensity modulated EHF EMR, presumably, manipulating by connected systems of enzyme reactions.

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[Millemetre waves inhibit the synergistic effect of calcium ionophore A23187 and phorbol ester in neutrophil respiratory burst].

The effect of extremely high frequency electromagnetic field (mm-waves) on respiratory burst of neutrophils was studied. The peritoneal evoked neutrophils of the mice (NMRI line) were used. The production of reactive oxygen species was estimated by luminol-dependent chemiluminescence technique. Cells were irradiated by the mm-waves of 41. 95 GHz in the far field zone of the channel radiator during 20 min. Absorbed energy flux density was 150 microW/cm2. The irradiation was carried out at different concentrations of calcium ionophore A23187 and then neutrophils were stimulated by phorbol 12-myristate 13-acetate (PMA) 1 microM, activator of PKC. At irradiation of neutrophils the synergistic action of A23187 and PMA was not changed at low concentration of ionophore 10 nM-0.5 microM and was suppressed at high concentrations 0.5-10 microM. The largest inhibition of about 60% was obtained at the concentration of A23187 20 microM. The effect of mm-waves was not found under exposure in Ca(2+)-free medium for all used A23187 concentrations. We suggest that the mm-wave effect on the production of reactive oxygen species by neutrophils is determined by the influx of extracellular Ca2+ and PKC.

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[Properties of the catalytic center of a secretory 28kDa protein (1-cys peroxiredoxin) from rat olfactory epithelium].

The secretory 28 kD protein, an abundant water-soluble protein from rat olfactory epithelium, belongs to the 1-Cys subfamily of thiol-specific antioxidants (peroxiredoxins). The 28 kD protein contains a single cysteine residue at the position 46 which accounts for the antioxidant activity. Here we studied the effects of N-ethyilmaleimide and t-butyl hydroperoxide on the antioxidant activity of the 28 kD protein and that of the 23 kD protein from rat erythrocyte which is a member of 2-Cys subfamily of peroxiredoxines. N-ethylmaleimide, modifier for cysteine residues, had no effect on antioxidant activity of the dithiothreitol-treated 28 kD protein but irreversibly inhibited activity of the 23 kD protein under reducing conditions. The 28 kD protein was sensitive to treatment with peroxides: t-butyl hydroperoxide at micromolar concentrations was shown to irreversibly inactivate 28 kD protein. In the presence of dithiothreitol, the lower level of peroxide concentrations was required to inhibit 28 kD protein activity. The mechanism of this effect may be mediated through conversion of sulfhydryl group of 46Cys to oxidized states (46Cys-SO2H and 46Cys-SO3H). Antioxidant property of 23 kD protein was impaired by t-butyl hydroperoxide only in the presence of dithiothreitol. The concentrations of t-butyl hydroperoxide needed to affect the 23 kD protein were at least one order of magnitude higher than were required for the 28 kD protein inhibition. The given results suggest the essential differences between catalytic site of 28 kD protein and that of 2-Cys peroxiredoxins.

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