PubMed Health⌕ Search

Biomedical subjects

V A Fedin

Publications and source records attributed to V A Fedin.

8 recordsLinked to original sources
PubMed1982

[Structural reconstruction of chemo-sensitive biomembranes during the action of low molecular weight compounds using spin resonance].

Using the spin probe technique, the changes in the supramolecular structure of the central nervous system synaptic membranes and of olfactory hair membranes of Rana temporaria induced by low molecular weight organic substances of different chemical nature, were investigated. It was found that the membrane structures under study differ considerably in their sensitivity to chemical stimulation and in temporal kinetics of structural transitions. A correlation between physiological parameters of olfactory perception of the compounds used and the parameters of structural transitions in olfactory hair membranes was established. The interrelationship between the experimental data and chemoreception of odorants and mediators as well as the applicability of these preparations for membrane screening of biologically active substances are discussed.

Animals↗
PubMed1979

[Structural changes of synaptic membranes under the action of specific antisera using the spin probe technique].

The spin probing technique was used to study the interaction of preparations of rat cerebral cortex synaptic membranes with specific antisera. It was found that the fluidity of membrane matrix largely depended on the nature of physiological processes involving synaptic membranes in vivo. The supramolecular structure of synaptic membranes isolated from the brain of trained animals differed from that of controls. Differences in the properties of synaptic membranes were also revealed during their incubation with specific antisera. The data obtained are interpreted in terms of immunochemical theory of memory and training.

Animals↗
PubMed1976

[Study of the structural lability of biomembranes and their components by the fluorescent analysis method. IV. Kinetic characteristics of the binding of unsaturated fatty acids with bovine serum albumin].

By studying fluorescent parameters of ionic and neutral probes the kinetics of complex formation between the molecules of bovine serum albumin (BSA) and unsaturated fatty acids was investigated. The following regularities were observed: 1. Unlike the saturated fatty acids the unsaturated ones changed fluorescent parameters of the probes according to the cooperative mechanism, significantly decreasing the quantum yield values; 2. Temperature dependence of the fluorescence of both probe types in the complexes BSA -- oleic acid and BSA -- linole acid shows some bends at t=30--39 degrees C for which the lipid components is responsible.

Anilino Naphthalenesulfonates↗
PubMedDate not supplied

[Fluorescence analysis study of the lability of biomembranes and their components. III. Kinetics of complex formation between bovine serum albumin molecules and higher saturated fatty acids].

Kinetic peculiarities of the sorption of natural limited fatty acids on the molecules of bovine serum albumine (BSA) were studied by investigating fluorescent parameters of ionic (1-anilinonaphtalin-8-sulphonate-ANS) and neutral (N-phenyl-1-naphtylamine-PNA) probes. The following regularities were found: 1. The parameters which characterize the microsurroundings of both probes (quantum yield of fluorescence, the binding constant) did not change significantly during the sorption of the fattyn acids (laurinic, palmitinic and methyl ether of the stearinic acid). An exponential character of BSA fluorescent titration with fatty acids points to a competitive character of the relationship dye -- fatty acid for the binding sites in hydrophobic sacks of BSA. 2. The study of the character of the effect of solution ionic strength on the sorption of fatty acids showed that along with hydrophobic interactions the electrostatic interaction between carboxyl residues of fatty acids and charged protein groups also significantly contributed to this process. 3. Temperature relationship of AMS and PNA fluorescence intensity in the complex BSA -- laurinic acid correlates well with temperature relationship obtained from a pure protein system.

Fatty Acids↗
PubMedDate not supplied

[The effect of thyroliberin on the structural characteristics of rat erythrocytes].

The effect of regulatory peptide thyrotropin-releasing hormone (TRH) on the structure of the plasma membrane and morphology of rat erythrocytes was studied using a spin probe and scanning electron microscopy. EPR spectra of the spin probe introduced in the intramembrane space demonstrate that TRH at 10(-7) and 10(-3) M induces structural changes in the erythrocyte membrane. Scanning electron microscopy showed that introduction of TRH at 10(-11), 10(-7), and 10(-3) M in the erythrocyte suspension increased the proportion of discocytes as compared to the control. This effect is due to TRH-induced cell transformation in discocytes. The obtained data suggest that TRH affects the membrane structure and the morphology of erythrocytes, changes the functional activity of these cells and, thus, indirectly influences the rate of the oxygen supply to tissue.

Animals↗