[Mechanism of the effect of varying saturation of the rat organism with thiamine on membrane-bound succinate dehydrogenase activity].

The properties of the membrane-bound succinate dehydrogenase (SDH) of rat liver mitochondria were studied in the presence of thiamine excess and deficiency in the body. In acute oxythiamine B1-avitaminosis, the content of phosphatidyl choline in the mitochondria fell and SDH activity was suppressed. After incubation of such mitochondria with a sonicated phospholipid emulsion from egg yolk the activity of the enzyme virtually returned to control values. Incubation of the mitochondria from control rats and animals given thiamine contained by phospholipid emulsion did not affect SDH activity.