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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Rouer, E., Rouet, P. & Leroux, J.P. Aldrin epoxidase activity in liver microsomes from normal or streptozotocin-diabetic rats: Comparison with activity in isolated hepatocytes from normal rats incubated with glucagon. Biosci Rep 7, 129–133 (1987). https://doi.org/10.1007/BF01121876
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DOI: https://doi.org/10.1007/BF01121876