RT Journal Article
SR Electronic
T1 Pyridine Nucleotide-Dependent Electron Transport in Kidney Cortex Microsomes: Interaction with Desaturase and Other Microsomal Mixed-Function Oxidases
JF Molecular Pharmacology
JO Mol Pharmacol
FD American Society for Pharmacology and Experimental Therapeutics
SP 60
OP 69
VO 13
IS 1
A1 MARK R. MONTGOMERY
A1 DOMINICK L. CINTI
YR 1977
UL http://molpharm.aspetjournals.org/content/13/1/60.abstract
AB Rat kidney cortex microsomes contain both cytochrome b5 and its flavoprotein reductase, yet do not catalyze fatty acyl-CoA desaturation. This inactivity was unaltered by feeding a high-carbohydrate diet. However, supplementation of liver or lung microsomes with kidney microsomes produced a significant increase in desaturase activity. Kidney microsomes had no effect on liver N-demethylation or aromatic p-hydroxylation and only an additive effect on aryl hydrocarbon hydroxylase activity, suggesting specificity for the kidney-dependent synergism of desaturase. Although stearoyl-CoA is not desaturated by kidney microsomes, it did inhibit both kidney aryl hydrocarbon hydroxylase activity and NADH-cytochrome c reductase activity, which was restored to the control level by cyanide; stearic acid had no effect on reductase activity. These results suggest the presence of a desaturase electron transport system in kidney which may lack a factor(s) normally present in liver and lung.