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Biomedical subjects

D N Ostrovskiĭ

Publications and source records attributed to D N Ostrovskiĭ.

At least 37 records · Page 2Linked to original sources
PubMed1980

[Proteolysis as an approach to the study of protein distribution in the membrane of Micrococcus lysodeikticus].

Treatment of M. lysodeikticus protoplasts with subtilisin or pronase did not affect their permeability and led to a digestion of 20--30% of protein. DS-Na electrophoresis of protoplast membranes resulted in disappearance of three protein bands. This suggests that the outer surface of M. lysodeikticus protoplasts contains three proteins other than respiratory chain enzymes, which are subjected to an attack by proteinases. Treatment of the M. lysodeikticus membranes, isolated by osmotic shock, with proteinases resulted in a digestion of 20--50% of protein. The factors preventing the interaction between the membrane components (e.g. decrease of Mg2+ concentration, ultrasound, KCl, EDTA and particularly detergents) favoured the proteolysis; however, the bulk of the proteins remained insensitive to the effect of proteinases. The membranes pretreated with DS-Na or chlorophorm--methanol mixture proved to be good substrates for proteinases. Treatment of the membrane fraction with proteolytic enzymes allowed to obtain some data on localization of respiratory chain enzymes in the membrane stroma of M. lysodeikticus. Thus, cytochrome c is localized nearer to the membrane surface than cytochromes a and b, while malate dehydrogenase is plunged deeper into the membrane stroma as compared to NADH dehydrogenase.

Cell Membrane↗
PubMed1979

[Bacterial membrane proteins. Properties of Micrococcus lysodeikticus NADH dehydrogenase].

NADH dehydrogenase was isolated from M. lysodeikticus membranes with FAD as a prosthetic group. It was found the enzyme molecular weight is about 140000 in 0,01 M phosphate buffer, pH 7,4 in 1% Triton X-100. The enzyme molecules are dimers consisting of two subunits with molecular weight of 70000. The content of alpha-helical regions is 30%, that of beta-forms is 13%. The protein globule is cross-linked with the disulfide bonds and has hydrophobic regions on its surface.

Cell Membrane↗
PubMed1979

[Compartmentation of gramicidin 5 in membranes of sensitive bacteria and protein-lipid interactions].

Gramicidin S is sorbed on the isolated membranes of granicidin-sensitive Micrococcus lysodeikticus strain. The antibiotic inhibits the membrane malate dehydrogenase within the temperature range of 9--42 degrees C, i.e. under conditions of gel and liquid-crystalline lipid state; however its effect at 10 degrees C is 10 times as low as is observed at 42 degrees C. The inhibitory effect of gramicidin S on malate dehydrogenase can be eliminated and the antibiotic can be removed from the membrane by an excess of different phospholipids. No transfer of the membrane components on exogenous phospholipids is observed. A prolonged (about 2 hrs, 30 degrees C) incubation of the membranes with gramicidin S results in irreversible inactivation of malate dehydrogenase, although the antibiotic can be still eliminated by an addition of phospholipid emulsions. It is suggested that gramicidin S forms complexes with phospholipids, in which the antibiotic is oriented to water. These complexes disturb the lipid-protein interactions, resulting in relaxation of the binding between the boundary phospholipids and proteins, in the loosening of near-protein lipid zones and simultaneous condensation of acid phospholipids in the whole membrane. Destruction of the lipid zone is accompanied by changes in the enzyme activity, by separation of lipid and protein regions and by transphase enzyme transitions (expulsion or immersion). A slow formation of secondary protein-protein associates may be irreversible.

Cell Membrane↗
PubMed1978

[Has the respiratory chain of Micrococcus lysodeiktocus any redox components on the outer surface of cytomembrane?].

M. lysodeikticus protoplasts have catalyzed the reduction of 5.10(-4) M ferricianide by endogenous substrates if the respiratory chain is inhibited by cyanide or anaerobiosis. A disturbance of the protoplast permeability by osmotic shock or Triton X-100 treatment resulted in the decrease of the endogenous ferricianide reduction rate and in simultaneous stimulation of malate ferricianide reductase activity in dehydrogenase site of the inner membrane surface. Reactivation of endogenous ferricianide reduction by protoplasts and the loss of malate stimulating activity were observed in hyperosmotic medium. Unlike malate oxidation by osmotically shocked protoplasts, endogenous protoplast repiration was resistant to ferricianide 5.10(-4) M). The latter, being added to protoplasts, induced the oxidation of anaerobically reduced cytochromes b556+560, and it practically did not affect cytochromes c552 and a601. The data obtained suggest that at least one of the respiratory chain components is arranged on the outer side of the protoplast membrane. This component is probably located in the cytochrome region. The results obtained confirm the hypothesis on transmembrane organization of the respiratory chain in M. lysodeikticus.

Cell Membrane↗
PubMed1977

[Variation of cell membrane lipid composition by means of lipid transfer proteins. Properties of the protoplast membrane of Micrococcus lysodeikticus after incorporation of phosphatidylcholine].

After incorporation of phosphatidylcholine (PC) into the protoplast membrane of M. lysodeikticus by protein mediated transfer from PC liposomes, the activity of some membrane bound respiratory chain enzymes was studied. It was found that incorporation of PC decreases the rates of oxidation of exogenous substrates (NADH, malate) but the level of endogenous respiration was not changed. Ferricyanidreductase activity of ghosts of M. lysodeikticus was not dependent upon the PC content of protoplasts. PC containing protoplasts showed a higher osmotic stability than unmodified protoplasts. It is concluded that the incorporation of PC into the protoplasts results in resealing, i. e. in the repair of local defects in the protoplast membrane.

Cell Membrane↗
PubMed1977

[Membranes of bacteria and mechanism of action of the antibiotic gramicidin S].

The cyclopeptide antibiotic gramicidin S taken at a concentration of 100--200 mkg/mg membrane protein rapidly increases the permeability of M. lysodeikticus protoplast membranes for substrates of respiratory chain and exogenous cytochromes c. Prolonged incubation of gramicidin S with protoplasts results in their lysis which is more fast at low temperatures. In contrast to natural gramicidin, a derivative of gramicidin S with acetylated amino groups does not inhibit either the micrococcus membrane dehydrogenase or the whole of respiratory chain and does not affect the osmotic barrier of protoplasts. Aliphatic diamines (at concentrations up to 0.1 M) and Ca2+ ions (10(-2) M) do not affect the functioning of the respiratory chain in isolated micrococcus membranes. Another derivative of the antibiotic with an increased distance of loaded amino groups from the cyclopeptide framework (diglycyl gramicidin S) affects the membrane in a way similar to that of natural gramicidin. Washing of gramicidin-treated membranes with NaCl enhances the inhibitory effect of the antibiotic on membrane enzymes. The data obtained suggest that in addition to ionic interactions some hydrophobic interactions also occur during gramicidin S binding to the bacterial membrane, probably at the expense of a hydrophobic peptide ring. It is assumed that gramicidin S, similar to Ca2+ and some other membranotropic agents provides for phase separation of negatively charged phospholipids from other groups of phospholipids, manifesting itself in an appearance of "frozen" sites on the membrane which destroys its barrier properties. This is due to the formation of ionic bonds of negatively charged phospholipids. Simultaneously, unlike Ca2+, gramicidin S, when interacting with membrane proteins, prevents their redistribution in more liquid parts of the membrane, which results in a situation when the respiratory enzymes become surrounded by alkyl chains with restricted motion.

Bacteriolysis↗
PubMed1976

[Study of the membranes of pigment-free mutant of Staphylococcus aureus].

The membranes from pigmented strain of Staphyloccus aureus 209-P and its apigment mutant B-6 were isolated. The infrared spectra, the cytochrome content, and the activities of the dehydrogenases and oxidases of the membranes were studied. The apigment mutant membranes differed from those of the pigmented strain in all parameters studied. It is concluded that the carotenoid pigments affect the chemical composition and functional activity of the Staphylococcus membranes.

Carotenoids↗
PubMed1976

[Change in lipid-protein interactions in the membranes of bacteria exposed to gramicidin S].

Effect of cyclopeptide antibiotic gramicidin S on some enzymes and physical state of isolated Micrococcus lysodeikticus membranes is studied. Malate and lactate dehydrogenases were monotonously inhibited under the increase of gramicidin S concentration, while the activity of NADH-dehydrogenase firstly decreased and then reversed to the initial level under further increase of gramicidin S concentration. The oxygen uptake under oxidation of NADH and malate with membranes almost completely inhibited by the antibiotic, while the activity of ascorbate-TMPD-oxidase activity slightly inhibited by the same concentration of gramicidin. The addition of Triton X-100 completely eliminated the inhibitory effect of gramicidin on malate dehydrogenase. The introduction into the membrane of spine probes (2,2,6,6-tetramethyl-4-palmitoylamidopiperidine-1-oxile and 2(14-carboxytetradecyl)-2-ethyl-4,4-dimethyl-3-oxyazolidinyloxile) revealed that gramicidin caused the condensation of membrane lipid component. It is suggested that ionic interaction of gramicidin S with membrane phospholipids brings to "a freezing" of lipids which is a direct cause of impairing the activity of membrane respiration enzymes and the change of their position in the lipid matrix, thus inhibiting energy-producing processes in cell.

Ascorbate Oxidase↗
PubMedDate not supplied

[Interaction of bacteria with mercuric compounds].

We investigated the interaction of mercuric compounds with the bacteria Corynebacterium ammoniagenes, Micrococcus luteus, and Mycobacterium smegmatus capable of producing hydroxylamines (R-NOH) and 2-C-methyl-D-erythritol-2,4-cyclopyrophosphate (MECP), which are prone to form free radicals. The interaction of these substances with Hg2+ ions and their dynamics during the mercuric poisoning of bacteria was studied by EPR and NMR. Under stress conditions induced by lowering pH or generation of active oxygen species, the bacteria and, especially, their mutants with enhanced sensitivity to oxidative stress, were found to respond to exposure to 1-3 micrograms/ml HgCl2 and p-chloromercuribenzoate by a several-fold increase in their viability. The data obtained were interpreted in terms of the involvement of the sulfhydryl groups of bacterial surface proteins in this phenomenon. The interaction of bacteria with mercuric compounds may affect the pathogenesis of tuberculosis and other diseases.

Corynebacterium↗