Aldrin epoxidase activity in liver microsomes from normal or streptozotocin-diabetic rats: Comparison with activity in isolated hepatocytes from normal rats incubated with glucagon |
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| Authors: | Evelyne Rouer Patricia Rouet Jean Paul Leroux |
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| Affiliation: | (1) INSERM U-75, CHU Necker Enfants-Malades, 156 rue de Vaugirard, 75730 Paris, Cedex 15, France;(2) Present address: INSERM U15, C. H. U. Cochin Port-Royal, 28 rue du Faubourg, St Jacques, 75674 Paris, Cedex 14, France |
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| Abstract: | Aldrin epoxidase activity in liver microsomes from streptozotocin-diabetic rats is only 40% of that from normal rats. Epoxidation of aldrin has also been assayed in freshly isolated hepatocytes from normal rats. Addition of 10–7 M glucagon to the incubation medium leads to a decreased aldrin epoxidase activity. Owing to the previously reported phosphorylation of a purified cytochrome P-450 isozyme, it is postulated that the cytochrome P-450 dependent aldrin epoxidase may be regulated by a glucagon induced phosphorylation process. |
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| Keywords: | rat liver microsomes hepatocytes aldrin epoxidase diabetes glucagon |
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