RESUMO
The activity of the hepatic microsomal enzymes hexabarbital oxidase, aminopyrine demethylase, and p-nitrobenzoic acid reductase were determined in the chronically uremic rats, acutely uremic rats and controls. Plasma corticoid levels (corticosterone) were also measured in all groups. A significant reduction in the hepatic microsomal enzyme activity as compared to controls was observed in both groups, with the chronic group showing slightly greater reduction. Furthermore, while plasma corticoid levels were significantly elevated in both groups, the acute uremic group had plasma corticoid levels which were almost twice the levels found in the chronically uremic animals. The significance of these observations are discussed.
Assuntos
Microssomos Hepáticos/enzimologia , Uremia/enzimologia , Doença Aguda , Corticosteroides/sangue , Oxirredutases do Álcool/metabolismo , Aminopirina N-Desmetilase/metabolismo , Animais , Nitrogênio da Ureia Sanguínea , Doença Crônica , Hexobarbital , Masculino , Nitrobenzoatos , Oxirredutases/metabolismo , Proteínas/metabolismo , RatosAssuntos
Receptores de Droga , Antagonistas Adrenérgicos alfa/antagonistas & inibidores , Animais , Aorta/metabolismo , Isótopos de Carbono , Dibenzilcloretamina/antagonistas & inibidores , Epinefrina/administração & dosagem , Epinefrina/farmacologia , Técnicas In Vitro , Raios Infravermelhos , Fenoxibenzamina/metabolismo , Coelhos , Receptores Adrenérgicos , Análise Espectral , Fatores de TempoRESUMO
Transferrin is essential for the entry of iron into cells, but whether the entire iron-transferrin complex or only the iron enters is not known. Separation of the cellular from the interparticulate radioactivity is a common problem with such studies. By pelleting cells under oil, we have made precise measurements of the uptake capacity for 59Fe of mouse lymphoma RI cells. At 37 degrees C an 18-fold concentration of iron was observed within 30 min; at 0 degrees C this value was about 3-fold. At 37 degrees C a maximum of 18,000 molecules of 125I-labelled Fe-transferrin were bound to each cell; this was reduced by about half at 0 degrees C. At 37 degrees C about 10,000-12,000 binding sites for 125I-apotransferrin were detected on each cell. From our data we conclude that although essential for the transport of iron, it is unlikely that transferrin enters RI cells. It is possible that iron is actively transported and that the receptor population is heterogeneous.