Publications by authors named "Korets'ka N"

The subunit organization and regulatory features of extracellular sialic acid specific lectin produced by saprophytic strains Bacillus subtilis IMV B-7014 have been investigated. Autofocusing method was used to identify three lectin isoforms that were distinguished by physicochemical and biological properties. Using the transcription system in vitro it was established that one of the targets of bacterial lectin action was DNA-dependent RNA-synthesis.

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The ability of natural and mutant Bacillus subtilis cultures with imperfect reparation/recombination system to synthesis of extracellular and surface lectins was investigated, and dependence of lectin production process on cultures' genotype was proved. Mutant B. subtilis recP has practically lost its ability to produce the extracellular lectins as a result of mutation of a gene of the reparation/recombination system.

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Isolation of lectins from extracts of the Sambucus nigra inflorescences and of pollen material have been performed using isoelectric focusing without carrier ampholytes (autofocusing). Fractions active in agglutination tests with different carbohydrate specificity were subjected to SDS-PAGE. The major lectin found in whole inflores-cences was GalNAc specific and is proposed to be a heterotetramer with subunits of about 30 and 33 kDa.

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The idea of the work was to study a combined effect of some lectins (Con A, PHA, STA, WGA, SNA, VAA) and new composite bioregulators (PhCA-1 and azapyrimidine derivatives) on growth of Bacillus subtilis cells in order to elucidate cell targets sensitive to lectin's activity. Study of combined effects of high- and low-molecular bioregulators may also be the subject of practical interest with a prospect of obtaining new bacterio-and carcinostatic drugs. Using B.

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The ability of Bacillus subtilis exolectin to modulate the effect of antibiotics acting as metabolic inhibitors, which can suppress the biosynthesis of cell wall glycans (ampycillin), replication (mitomycin C) and transcription (rifampycin), have been investigated on mutants of B. subtilis. Extracellular lectin was produced by B.

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Using the bacterium B. subtilis as a model and antibiotics as metabolic inhibitors which can suppress replication (mitomycin), transcription (rifampycin) or translation (streptomycin), it is shown that carbohydrate-binding proteins (lectins of plant origin) have different action on intracellular processes under study. The effect depends on lectin's structure and on the condition of bacterial reparation/recombination system.

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