Glycogen synthesis in isolated perfused livers or livers of anesthesized rats (in situ), was studied using radioactively labelled fructose, lactate, and inositol as substrates. The specific radioactivity of glucose and glycogen was measured at various times and compared with that of some intermediates. The results suggest that liver glycogen is formed from the pool of free glucose which in turn is fed by the so-called "direct and indirect pathway" of glycogen synthesis.
View Article and Find Full Text PDFRats were treated for 5 to 14 days with perfluoroacetate, perfluorobutyrate and perfluorooctanoate. Alterations in hepatic morphology with special reference to the peroxisomal compartment were investigated by light and electron microscopy following cytochemical staining of catalase activity with the alkaline 3,3'-diaminobenzidine medium. All three compounds induced hepatomegaly and peroxisome proliferation.
View Article and Find Full Text PDFTwo different peroxisome preparations were isolated from male rat liver by using total homogenate (TH) as the starting material for one and the light mitochondrial (L) fraction for the other. The technique worked out is based on rate zonal (RZ) centrifugation in a sucrose gradient and subsequent isopycnic centrifugation in a Nycodenz gradient. The peroxisome fraction isolated from the L fraction consisted of 97-98% peroxisomal protein with catalase activity 49-fold enriched over TH.
View Article and Find Full Text PDFThe paper presents results that a hyperthyroid state for 5 to 10 days induces a new peroxisome population in the liver of male rats. This assumption is based on the following observations: 1. Treatment of male rats for five consecutive days with 25 micrograms thyroxine per day resulted in an increase of catalase and D-amino acid oxidase activities by 32 and 61%, respectively.
View Article and Find Full Text PDFEur J Cell Biol
October 1980
Polyamines are associated with fundamental metabolic and functional steps in cell metabolism. The activity of ornithine decarboxylase, the key enzyme in polyamine metabolism, was followed during the preparation of rat liver parenchymal cells and in the isolated cells during incubation. In experiments in which ornithine decarboxylase was not induced in vivo, enzyme activity dropped to barely measurable values during the preparation.
View Article and Find Full Text PDFCytobiologie
December 1978
Rat liver ornithine decarboxylase activity was measured during phalloidin poisoning of 17 day-old rats, adult rats, and adult rats protected against phalloidin toxicity by pretreatment with somatotropin. The results show: 1. In adult rats, after a short period of activation, ornithine decarboxylase activity decreases to basal levels after phalloidin administration and remains so until death.
View Article and Find Full Text PDF1. Somatotropin protects rats against a lethal dose of phalloidin (1.3 mg/kg).
View Article and Find Full Text PDF1. The uptake, binding and elimination of phalloidin in liver is compared in adult (180 to 240 g) and "baby" (17 to 19 days old) rats in vivo and in vitro. 2.
View Article and Find Full Text PDFHoppe Seylers Z Physiol Chem
October 1974