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

Jpn J Pharmacol. 1983 Oct;33(5):999-1006. doi: 10.1254/jjp.33.999.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cytochrome P-450 Enzyme System / analysis*
  • Hydroxylation
  • Kidney / metabolism*
  • Lauric Acids / metabolism*
  • Male
  • Microsomes / metabolism*
  • Microsomes, Liver / metabolism*
  • Molecular Weight
  • Oxidation-Reduction
  • Rats
  • Rats, Inbred Strains
  • Starvation / metabolism*


  • Lauric Acids
  • lauric acid
  • Cytochrome P-450 Enzyme System