Publications by authors named "L Sibeldina"

High-resolution 1H-NMR spectrometry (360 MHz) was used in combination with thin layer chromatography to study changes in composition and molecular structure of inverted micelles of blood lipids from patients with breast and uterus cancer. Changes in relative intensity of NMR signals of lipids compared with norm were revealed. The changes in the lipid composition of blood components, in particular, in cholesterol content, determine the differences in structure and molecular mobility of these lipids, which probably explains the regularities observed in the NMR spectra.

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Chemical shifts in 31P-NMR spectra of linear polyphosphates were studied. In each polyphosphate species tested, the sum of signal intensities of the internal (core) phosphate groups was proportional to the concentration of each polyphosphate, but the contribution of such groups to the total intensity of the signal decreased with increasing the length of the polyphosphate chain. An equation for estimating the polyphosphate chain length in biological objects taking into account a decrease in the 31P-NMR spectral intensity is proposed.

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The dynamics of the content and the degree of polymerization of polyphosphates (PPs) during the growth of Saccharomyces cerevisiae VKM Y-1176 was studied by chemical methods and P NMR spectroscopy. The overall PP content of Saccharomyces cerevisiae cells growing in orthophosphate-sufficient medium was found to increase until glucose was exhausted in the medium. In the early logarithimic phase, the degree of polymerization of PPs (high-polymeric PPs in particular) fell drastically.

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2-C-methyl-D-erythritol-2,4-cyclopyrophosphate (MEC) identified as a new bacterial oxidative stress substance (Ostrovsky D. et al. (1993) Biochem.

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Data on 32P-label incorporation with subsequent addition of non-radiolabelled o-phosphate suggest that the new phosphorus compound, 2-C-methyl-D-erythritol-2,4-cyclopyrophosphate (MEC), accumulated in the cells of some bacterial species in response to oxidative stress does not rapidly exchange phosphorus with external o-phosphate 3 hours after the introduction of its synthesis inducers into the Corynebacterium ammoniagenes culture. The accumulated MEC is retained in the cells despite the action of the cell wall synthesis inhibitor, chloramphenicol, or the energetic poisons, KCN and iodoacetate and also under anaerobic conditions. It has been shown that incubation of the cell-free lysate of a non-induced culture, Micrococcus luteus, with MEC does not result in MEC hydrolysis; therefore, MEC accumulation after the redox-mediator addition is hardly due to the hydrolase inactivation but, rather, is due to the activation of the MEC-synthesizing enzyme.

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