[Denaturation changes in the proteins of the membrane structures of the brain during deprivation of the paradoxical stage of sleep].

24--96-hour REM-sleep deprivation entailed a rise of SH-group content in the proteins of the rat diencephalon and mesencephalon tissue homogenates, whereas SH-group content of the homogenates of the cortex, pons with medulla oblongata, and cerebellum remained unchanged. Neither did the content of SH-groups change in the soluble protein fraction nor the content of low-molecular thiol substances in the brain parts under study. From among the subcellular fractions of the brain-stem homogenate, the increase of SH-group content after 24-hour REM-sleep deprivation occurred in the synaptosomal and nuclear fractions but not in the mitochondrial one. The REM-sleep deprivation did not affect the --S--S-group content in these fractions. In the anterior parts of the brain-stem only REM-sleep deprivation led to conformational changes of structural proteins towards their denaturation but without rupture of the disulfide bonds.