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Biomedical subjects

D A Turgenbaeva

Publications and source records attributed to D A Turgenbaeva.

5 recordsLinked to original sources
PubMed1981

[Structure of the Micrococcus lysodeikticus respiratory chain using low concentrations of Triton X-100 and glutaric aldehyde].

Using low (0.0025 -- 0.025%) concentrations of Triton X-100, the correlation between the decrease of NADN- and malate oxidase activities and NADH- and malate dehydrogenase release in large fragments of Micrococcus lysodeikticus membranes was established. This was accompanied by membrane suspension clearance and a decrease of microviscosity of the membrane lipid component. Using NADH-dehydrogenase, it was shown that the attachment of NADH-dehydrogenase to the membrane treated with glutaric aldehyde occurs in two steps, this being indicative of different environment of this enzyme in the membrane. The data obtained are discussed in terms of laterally heterogenous structure of the bacterial membrane with respect to the electron transport enzymes, in particular in favour of an existence of individual sites of the membrane containing dehydrogenases rather than other respiratory chain components.

Alcohol Oxidoreductases↗
PubMed1979

[Cytochrome b556 complexes solubilized from Micrococcus lysodeikticus membranes by triton X-100].

The integral protein of cytochrome b556 after its solubilization with Triton X-100 from M. lysodeikticus membranes was studied. The cytochrome was found in complexes differing in charge and size during preparative gel electrophoresis and centrifugation in a sucrose concentration gradient. Cytochrome b556, being in complexes, retains its ability to be reduced by NADH dehydrogenase. The electron micrographs of the membranes after solubilization by Triton X-100 demonstrated the maintenance of the membrane structure. It is concluded that native protein complexes marked with cytochrome b556 are extracted from the membranes under their solubilization.

Centrifugation, Density Gradient↗
PubMed1979

[Study of membrane proteins from Microccus lysodeikticus using immunochemical methods].

Using immunoelectrophoresis, the antigenicity of various protein fractions of the Micrococcus lysodeikticus membranes was evaluated. It was shown that both the peripheral and integral membrane proteins possess the antigenic determinants. The antiserum exhausted by the M. lysodeikticus mebranes loses its ability to interact with intergral proteins, which are not solubilized by Triton X-100. It was thus assumed that the integral proteins are exposed on the membrane surface constantly or periodically and that there exist no proteins which are completely and permanently incorporated into the lipid bilayer. The respiratory chain of the M. lysodeikticus membrane is inhibited by membrane immunoglobulins by 50%. This is probably due to the presence in the membrane antiserum of antibodies specific to the respiratory chain enzymes. Evidence for this assumption can be derived from the fact that partially purified cytochrome b556 forms a precipitation zone with the membrane antiserum and that the activity of membrane NADH-dehydrogenase is inhibited by a monoserum against NADH-dehydrogenase.

Cell Membrane↗
PubMedDate not supplied

[Action of the steroid glycoside deltonin on the bacterial membranes of Micrococcus lysodeikticus].

A slight detergent-like effect of steroid glycoside deltonine from Dioscorea deltoidea on the bacterial membranes of Micrococcus lysodeikticus was detected which resulted in the breaking of the osmotic barrier of protoplasts and in the loss from the membranes of small fragments containing the dehydrogenases of the respiratory chain but without cytochromes. These small fragments still retained the membrane structure.

Cell Membrane↗