[Genetic determination of the neurophysiological mechanisms of the cortico-subcortical integration of bioelectrical activity of the brain]. / Geneticheskaia obuslovlennost' neirofiziologicheskikh mekhanizmov korkovo-podkorkovoi integratsii bioélektricheskoi aktivnosti mozga.

Contribution of genetical factors to neurophysiological mechanisms of cortico-subcortical integration was investigated in 12 pairs of the monozygotic and 5 pairs of dizygotic twins (aged from 18 to 25). In each pair of twins as well as in all 544 unrelated pairs of subjects from both groups, interpairs similarity of the character of the spatial interaction of bioelectrical activity of the neocortex for different combinations of statistical correlations of EEG (from 16 monopolar electrodes) was estimated. The data obtained allow to suggest a higher common population invariance and a relatively small hereditary and phenotypic variability of morphofunctional systems, which underlie neurophysiological mechanisms of the brain integration in general. Apparently, the formation of the brain stem and subcortical regulatory structures in the ontogenesis, the structures that play the main role in the realization of system combination of different parts of the brain into united formation, occurs to all individuals according to a single principle since its disturbance can probably affect the fundamental monomorphal features of the species. In turn, one can expect a great interindividual variability of establishing of the intraregional connections of neocortex, the role of genetic and environmental factors in the formation of short and relatively long interactions being complex.

[Display of activities of integrative brain mechanisms in its bioelectrical activity]. / O proiavlenii deiatel'nosti integrativnykh mekhanizmov mozga v ego bioélektricheskoi aktivnosti.

Integrative processes taking place in CNS lie in the basis of the activity of the whole brain, i.e. they perform as a system-creating factor; they maintain the system stability, succession of its functioning, regularity of intra-system connections and their reproduction. Can this activity appear in extremely mobile, polyform EEG processes? The results of EEG factor analysis show the existence of the very stable uniform structure of spatial interactions of cortical potentials. This structure can be reproduced from EEG of different adult individuals, as well as of children at various stages of ontogenesis. EEG from any point of the cortex can be represented as a linear combination of only three orthogonal components. These components are the same for all the cortical regions. Especially local, independent fluctuations in EEG constitute less than 10% for adults and not more than 20% for newborns. Apparently, the continuous reflection of oscillations of the whole biopotential field in any point of the cortex reveals in EEG the functioning of a mechanism providing the activity of the brain as a whole.

[Isolation of (ADP-ribose)polymerases from the calf testis and thymus and comparison of their basic physico-chemical properties]. / Vydelenie (ADP-riboza)polimeraz iz semennikov i timusa byka i sravnenie ikh osnovnykh fiziko-khimicheskikh svoistv.

Highly purified preparations of (ADP-ribose) polymerase were obtained from calf testis and thymus by chromatography on DNA-cellulose, hydroxyapatite and gel filtration. It was shown that the enzymes isolated from both sources under identical conditions have similar values of Mr, Vmax and Km in the reactions of autoribosylation and poly(ADP-ribosylation) of histone H1 as well as similar pH-dependencies of the catalyzed reactions.

[Bovine liver glutamate dehydrogenase modified by 2,2,6,6-tetramethyl-4-oxopiperidine-1-oxyl: enzymatic activity and catalytic properties]. / Modifikatsiia glutamatdegidrogenary pecheni byka 2,2,6-6-tetrametil-4-okso-piperidin-1-oksilom. Vliianie na aktivnost' i kataliticheskie svoistva.

When modified by 2,2,6,6-tetramethyl-4-oxopiperidine-1-oxyl (TMPO) bovine liver glutamate dehydrogenase (L-glutamate NAD(P) oxidoreductase, E. C. 1.4.1.3) looses its catalytical activity and sensitivity to allosteric inhibitor GTP. The stoicheiometry of the binding of TMPO to glutamate dehydrogenase has been studied--each protomer bound one molecule of TMPO. It is supposed that TMPO reacts with lysine residue located in the enzyme's active center.