In order to elucidate the intrahepatic metabolism of Sulfobromophthalein (BSP), the fate of administered BSP was observed in the blood, Iiver and bile of rats or dogs under several conditions.
The results were as follows;
1) In normal rats, BSP disappeared rapidly from the plasma, while in the rats with carbon tetrachloride intoxication a large proportion of BSP retained in it. As compared with the control group the CCl4 group showed an increased content of unconjugated BSP in the liver. The concentration of BSP inthe bile of the CCl4 group decreased, indicating a reduced excretion of conjugated BSP.
2) Hepatic BSP, analyzed by gel filtration method using Sephadex G_100 or G_25, consisted of the protein bound and protein unbound type. The protein bound and the protein unbound BSP were further characterized by paper electrophoresis as the unconjugated and the conjugated BSP. The protein bound BSP was proved to be overwhelmingly the unconjugated BSP and the protein unbound BSP to be the conjugated BSP. An addition of reduced glutathione to the supernatant fraction of rat liver in vitro, caused an increase of the protein unbound BSP. PCMB, known to be the inhibitor of SH-enzymes, was proved to inhibit, also, the conjugation of BSP with GSH in vitro. These findings suggest that the conjugating mechanism of BSP participates in the release of BSP from liver cell supernatant.
3) Following incubation of rat liver slice with BSP solution, the concentration of BSP in the medium decreased and the conjugated BSP appeared. Using the liver slice treatedwith CCl4 or PCMB, the decrease of the unconjugated BSP in the medium was inhibited. It was suggested that the uptake of BSP by liver slce is disturbed by the treatment with CCl4 or PCMB
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