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End date: 1999Subject: search.filters.subject.Bacillus subtilis

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    Secretion patterns of proteins of Bacillus subtilis grown with Triton X-100 and n-octyl-beta-D-glucopyranoside
    (1987) Baykousheva, S; Ilieva, K
    (Reproduced from SciFinder, with permission from the Chemical Abstracts Service) The effect of two membrane-active agents, Triton X-100 and n-octyl-beta-D-glucopyranoside, on B. subtilis 168 was studied. When present in the growth medium, the detergents decreased the extracellular proteolytic activity. The electrophoretic patterns of proteins in the presence or in the absence of these agents differ significantly.
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    Electron-microscopic demonstration of the localization of adenosinetriphosphatase in Bacillus subtilis
    (1984) Cherepova, N.; Baykousheva, S.; Ilieva, K.
    Histochemical studies and electron microscopy of Bacillus subtilis revealed the presence of ATPase in various subcellular fractions. The enzyme was preferentially localized in mesosomes, cytoplasmic membrane, periplasmic space, and cell wall.
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    Suppression of serine protease secretion and sporulation in Bacillus subtilis by detergents
    (1987) Baykousheva, S.; Ilieva, K.
    In Bacillus subtilis grown under aeration at 37° for 24 h in liquid nutrient medium containing the nonionic detergents octylphenol-polyethylene glycol ether or polyoxyethylene monocetyl ether, increasing the concentrations of the detergents led to a decrease in the amount of protease secreted from the cells and abolished sporulation. Possible mechanisms by which these detergents caused these actions are discussed.
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    Ultracytochemical localization of ATP-hydrolysing activity in vegetative cells, spores and isolated cytoplasmic membranes of Bacillus subtilis 168
    (1986) Cherepova, N. V.; Baykousheva, S. P.; Ilieva, K. Z.
    The localization of ATP-hydrolysing activity in vegetative cells, spores and isolated membranes of Bacillus subtilis 168 was studied by a cytochemical method combined with electron microscopy. The activity was located mainly in the cytoplasmic membrane and the mesosomes, and was also found in the inner layer of the cell wall facing the cytoplasmic membrane. Activity was also detected in the cross-membranes of dividing cells and in spore coats. The product of the reaction was observed either as fine electron-dense granules incorporated into the membranes, or as high-contrast lead precipitates on the surfaces of the membranes.
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    Secretion of proteins by Bacillus subtilis 168 grown in the presence of membrane active agents (alcohols)
    (1988) Baykousheva, S.
    Sodium dodecyl sulphate-polyacrylamide gel electrophoresis was used to study the composition of proteins secreted by the Gram-positive microorganism Bacillus subtilis strain 168 when the latter was grown in the presence of primary alcohols (methanol, ethanol, 1-propanol and 1-butanol). These membrane-active agents had different effects on the pattern of proteins exported by B. subtilis. The secretion of some proteins was inhibited by the alkanols while that of others was stimulated, depending on the type of drug used. All alcohols were found to decrease the activity of extracellular enzymes such as alpha-amylase and serine protease without affecting significantly the activity of these enzymes when tested in vitro. The observed effects might be due to the ability of these agents to perturb the structure of biological membranes, thus interfering with the process of protein translocation through the lipid bilayers.