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The examination was applied to enterprise workers laboring in conditions of vinyl chloride (79 patients), caustic soda (24 patients) and 10 patients with professional chronic mercury intoxication. The differences are established concerning manifestation of autoimmune reactions of personnel working in conditions of chronic effecting of vinyl chloride distinct of parameters characterizing autoimmune reactions of personnel working under impact of another neuro-toxicants (vapors of metallic mercury). The increasing of auto-antibodies to MAG was detected in healthy personnel and increasing of concentrations of auto-antibodies to protein S-100 and DNA was detected in personnel with initial manifestations of neuro-intoxication. These occurrences testify availability, of different mechanisms underlying formation of neurological disorders. The study data confirms involvement of auto-antibodies to neuronal antigens into derangement of neural activity in personnel working in conditions of effect of vinyl chloride and vapors of metallic mercury. Hence, the new possibilities are opened in studying pathogenesis of occupational neuro-intoxications. The detection of auto-antibodies to proteins of neural tissue can be recommended as a criterion of early identification of damage of neural system in personnel working in conditions of chemical industry.

The recombinant mts-1 protein has been obtained with the use of the pMAL-c expression vector. This protein was shown to bind calcium ions and interact with melittin, a polypeptide from bee venom.

Elaboration of alimentary conditioned reflex in rats is accompanied by an increase of the level of protein S-100 in the left and right cerebral hemispheres. Amnestic factor M-cholinolytic atropine disturbs the elaborated habit and simultaneously decreases the quantity of protein S-100 up to the level of unlearned animals. The elaboration of conditioned reflex of passive avoidance does not change the content of protein S-100 in the rats brain. Intracisternal injection of antiserum to protein S-100 has an expressed amnestic action. Intracisternal injection of protein S-100 against the background of amnestic action of cholinolytic does not lead to restoration of memory. The cholinolytic and antiserum to protein S-100 mutually potentiate the amnestic effect.

A procedure for preparative separation of proteins from bovine brain precipitated in a saturated solution by ammonium sulfate (pH 4.0) and remaining in the supernatant is described. It was shown that not less than 22 fractions (up to 28 fractions considering the "equivocal" reaction) produce different responses to the antiserum against the major protein, i.e. S100.

Six peptides (presumably products of natural protein S100 catabolism) were isolated from bovine brain extracts by hydrophobic chromatography, affinity chromatography on immobilized antiprotein S100 antibodies, gel filtration and chromatography on TSK HW-40 columns in a methanol: water system. At 10(-12) M, peptide AT-I-I caused a 70% inhibition of the specific binding activity of endogenous benzodiazepine brain receptors. When used at higher concentrations (10(-9)-10(-5) M), AT-I-I inhibited the binding activity of central serotonin, dopamine and m-cholinoreceptors. Immunochemical analysis revealed the presence of identical material in rat brain glial cell nuclei (astrocytes). Using a solid phase immunoenzymatic assay, it was shown that peptide AT-I-I was not identical to any other of the 14 peptides tested (commercial preparations). Data from immunochemical analysis testified to the species non-specificity of AT-I-I. It was concluded that in brain tissue natural proteolysis of proteins S100 leads to the formation of biologically active oligopeptide products that are involved, in particular, in the modulation of the functional activity of central benzodiazepine receptors.

The biospecific preparation and a preliminary analysis of physico-chemical properties of water-soluble proteins from bovine brain and liver and brain oligopeptides specifically adsorbed on a column with immobilized brain-specific proteins of the major fraction S100 were carried out. Using thin-layer electrophoresis on cellulose and tachyphoresis, it was found that four oligopeptide cations and three anionic oligopeptides interact with S100. Polyacrylamide gel electrophoresis revealed at least six brain proteins and 11 liver proteins, which interact with S100. An essential role in interaction of protein ligands from the bran (but not from liver) with immobilized S100 proteins belongs to Ca2+. The use of natural endogenous ligands for the study of the biological role of brain-specific proteins S100 is discussed.