Abstract
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.
- Copyright © 1977 by Academic Press, Inc.
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