Effects of starvation on microsomal cytochrome P-450 and laurate-omega-hydroxylation of rat kidney and liver.
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 one dimensional separation using peroxidase stained SDS-continuous gradient polyacrylamide gel electrophoresis. Gels of the hepatic microsomes treated with phenobarbital showed three P-450 bands, and the renal microsomes showed one 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. It seemed, therefore, that a special P-450 subunit catalyzing laurate-omega-oxidation 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.
D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000032:analysis*; D006900:Hydroxylation; D007668:Kidney / Q000378:metabolism*; D007850:Lauric Acids / Q000378:metabolism*; D008297:Male; D008861:Microsomes / Q000378:metabolism*; D008862:Microsomes, Liver / Q000378:metabolism*; D008970:Molecular Weight; D010084:Oxidation-Reduction; D051381:Rats; D011919:Rats, Inbred Strains; D013217:Starvation / Q000378:metabolism*
D007850:Lauric Acids; C030358:lauric acid; D003577:Cytochrome P-450 Enzyme System