Effect of reticular formation and hypothalamus on the cortical hemodynamics.
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Biomedical subjects
Publications and source records attributed to V V Suchkov.
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Data are presented concerning the effect of heating rate on the denaturation parameters of small and oligomeric globular proteins: Kunitz trypsin inhibitor from soybeans and 1,5-Ribulose Bisphosphate Carboxylase from tobacco leaves. Substantional dependence of denaturation temperature on the heating rate reflects non-equilibrium pattern of denaturation of these proteins under experimental conditions. To interpret these data a kinetic approach is proposed, which permits determination of equilibrium value of the denaturation temperature and of the constant of de- and renaturation rate. The conformation transitions in the proteins studied are shown to be relatively slow processes. Their rate is comparable to the velocity of temperature change in a calorimeter, which is the cause of non-equilibrium effects in a calorimetric experiment.
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The effect of prostaglandins (PG) E1, A1, and F2 alpha on the systemic arterial blood pressure, local brain circulation, vascular resistance and oxygen tension in the motor region of the cortex, reticular formation and ventromedial nucleus of the hypothalamus was studied in experiments on non-narcotizied rabbits. Intravenous administration of PGE1 (10 microgram/kg/min); PGA1 (50 microgram/kg/min) and PGF2 alpha (50 microgram/kg/min) produced systemic hypotension accompanied by reduction of the local brain blood flow, vascular resistance and oxygen tension in the cortex and subcortical structures. The most pronounced changes in the systemic arterial blood pressure and local brain blood flow were recorded after PGE1 administration, these changes being less marked after PGA1 and PGF2 alpha injections.
Concentration dependencies of maximum temperature (Td), thermal effect of denaturation (delta Qd) and also of glass transition temperature (Tg) were obtained in heat capacity investigation of five globular proteins with low water content. Special features of the observed Td and delta Qd dependencies, both general for polymers and specific for proteins, are discussed. The assumption is put forward that anomalously strong dependence of protein Tg on humidity, bringing together glass and denaturation transitions, results in the fact that denaturation process can be observed in completely dehydrated proteins. The denaturation parameters of dry proteins were determined.