Autor: |
Hutterer, Ferenc, Bacchin, Paolo G., Raisfeld, Ilene H., Schenkman, John B., Schaffner, Fenton, Popper, Hans |
Zdroj: |
Experimental Biology and Medicine; February 1970, Vol. 133 Issue: 2 p702-706, 5p |
Abstrakt: |
In cholestasis, 4 days after bile duct ligation, the activity of aminopyrine demethylase was greatly decreased, while the content of cytochrome P-450 and the activities of aniline hydroxylase, NADPH-cytochrome creductase, and cytochrome P-450 reductase were only slightly decreased in the microsomes of the rat livers. Binding of type II substrate to cytochrome P-450 was unimpaired and its modifier effect on P-450 reductase was intact. The binding of type I substrate was greatly decreased, and its stimulating effect on P-450 reductase was abolished, suggesting that the effect of cholestasis on the hepatocellular smooth endoplasmic reticulum is to alter the type I binding sites, which is responsible for the hypoactivity of the biotransformation system. |
Databáze: |
Supplemental Index |
Externí odkaz: |
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