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Biomedical subjects

K Dobrovský

Publications and source records attributed to K Dobrovský.

6 recordsLinked to original sources
PubMed1991

[Possibilities of therapeutic applications of neuronal calcium homeostasis].

The role of calcium as a second messenger which mediates the transmission of the signal and has an impact on cellular regulation of the majority of organs at all stages of development was confirmed during the past decade. In the submitted review the authors summarize mechanisms by which calcium exerts its regulatory function. At the same time the authors discuss the possible ratio of disorders in the above systems in various diseases in particular those of the central nervous system and possible pharmacotherapeutic interferences at different levels of transmission of the signal mediated by calcium. As in the mentioned area at the clinical level so far mainly calcium channel blockers were used, the authors summarize the use of these substances in the treatment of cerebral ischaemia, migraine, epilepsy and manic-depressive disease.

Animals↗
PubMed1989

Conformational stability of spectrin and fodrin.

The conformational stability of erythrocyte spectrin and brain spectrin-like protein (fodrin) has been studied by circular dichroism. In agreement with previous reports the circular dichroism spectra of both proteins in the peptide region were almost identical. The essential differences, on the other hand, were found in the near u.v. range, most probably due to differences in the conformation of intrachain disulphide bonds. Heat denaturation curves, relating to the level of secondary structure (ellipticity at 221 nm) showed that fodrin is more stable than spectrin: curves of reversible as well as irreversible denaturation are shifted to higher temperatures and also the amount of alpha-helices in the denatured state is higher. Spectrin conformation was found to be very sensitive to the presence of water-soluble organic solvents; the denaturation curves exhibit maxima and minima not typical of protein isothermic denaturation. The observed low conformational stability of spectrin is discussed in the context of its molecular environment and function in the red cell membrane.

Animals↗
PubMed1987

Structural analogy among mammalian spectrins and spectrin-like proteins revealed by molybdenum labeling.

Pentavalent complex of 99Mo with ascorbic acid binds in vitro to the plasma membranes of human, rabbit, rat and mouse red cell membranes and to bovine synaptic and rat intestinal brush border membranes. Red cell spectrins and spectrin-like proteins from non-erythroid cells were determined as the molybdenum-binding proteins in the membranes. Specificity of this binding among all membrane proteins suggests structural analogy in this group of proteins.

Animals↗
PubMed1982

Causes for rifampicin toxicity--experimental study.

A 12-day-experimental study of rifampicin (RMP) on male rats followed both the biochemical indices signalling disorder of metabolic equilibrium in the organism, and distribution of RMP in the tissues. The study showed the RMP concentration to be manifold higher in the liver than in the blood and other organs; in epididymal fat the concentration in one half of that in the blood. RMP adversely affects the energy metabolism, i.e. intake and resorption of nutrients, especially metabolically and calorically important lipids and sugars. RMP is harmful also for liver parenchyma.

Alanine Transaminase↗