[The sensitivity of the irradiated DNA of various bacteriophages (T4r, T7, lambda and B3) to a hydrodynamic shift].
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Bacteriophages↗
Biomedical subjects
V A Struchkov
Publications and source records attributed to V A Struchkov.
[Change in the supramolecular DNA-residual protein complex in the thymus and liver of gamma-irradiated rats].
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Amino Acids↗
[Various structural-functional states of DNA in animal cells before and after gamma-irradiation].
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Animals↗
[The mechanism of T2 and lambda phage DNA molecule double break formation when irradiated in solution and the radiobiologic role of these breaks].
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Coliphages↗
[The effect of free radicals on solutions of "super-polymer" desoxyribonucleic acid].
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Animals↗
[Study of the character of radiation injury of submolecular DNA using the method of hydrodynamic shift].
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Animals↗
[Radiosensitivity of single- and double-strand DNA solutions].
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DNA↗
[The role of single breaks in the mechanism of action of ionizing radiation on supramolecular DNA in the cell].
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Animals↗
[The role of disulfide bridges of the residual protein in chromosomal DNA organization].
The review of literature data and our investigation on the role of disulfide bridges of residual protein (RP) in structural organization of chromosomal DNA is presented. It was studied the action of several S-S cleaving agents (2-mercaptoethanol, dithiothreitol, NaBH4, glutathione reductase) on native DNA-RP complexes, isolating from the different eukaryotic and prokaryotic cells. It was shown, that the thiols result the fragmentation of DNA-RP complex in double-strand subunits of several size (5 x 10(5), (18-20) x 10(6), 70 x 10(6) Da) on dependence of the incubate condition (concentration of thiols, pH, time). It was observed, that specific S-S bonds (thiol-sensitivity at neutral or acid conditions, glutathione reductase-sensitivity) are present in DNA-RP complexes, which may control of different structural levels of DNA into chromosome (gen-transcription-replicon-domain). The possible quasisubunit structure of chromosomal DNA with participation of polypeptide S-S bonds and complementary "sticky" ends of subunits is discussed.
Animals↗