Aldrin epoxidase activity in liver microsomes from normal or streptozotocin-diabetic rats: comparison with activity in isolated hepatocytes from normal rats incubated with glucagon.
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.
D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism; D003921:Diabetes Mellitus, Experimental / Q000201:enzymology*; D005934:Glucagon / Q000494:pharmacology*; D008099:Liver / Q000166:cytology / Q000201:enzymology*; D008862:Microsomes, Liver / Q000201:enzymology; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D010766:Phosphorylation; D051381:Rats; D013311:Streptozocin
D013311:Streptozocin; D005934:Glucagon; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; C019647:aldrin epoxidase