Effects of starvation on microsomal cytochrome P-450 and laurate-.OMEGA.-hydroxylation of rat kidney and liver.

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Abstract
Cytochrome P-450 (P-450) content and laurate-.omega.-oxidation activity in rat kidney and liver microsomes were investigated following starvation. Multiple forms of P-450 were analyzed by 1-dimensional separation using peroxidase stained SDS-continuous gradient polyacrylamide gel electrophoresis. Gels of the hepatic microsomes treated with phenobarbital showed 3 P-450 bands, and the renal microsomes showed 1 sharp band, which was induced remarkably by starvation and coincided with the middle molecular form of P-450 from the hepatic microsomes. Since laurate-.omega.-oxidation activity was induced specifically by starvation but not by drug treatment, in both the kidney and the liver microsomes, the middle molecular form of P-450 might catalyze laurate-.omega.-oxidation. A speical P-450 subunit catalyzing laurate-.omega.-oxidation apparently has a greater function in the renal rather than hepatic microsomes because the specific laurate-.omega.-oxidation activity per starvation induced P-450 content was relatively similar in both the kidney and the liver.