Purification and properties of cytochrome P-450 from homogenates of human fetal livers

Arch Biochem Biophys. 1985 Aug 15;241(1):275-80. doi: 10.1016/0003-9861(85)90383-2.


A form of cytochrome P-450, namely P-450HFLa of human fetal livers, was purified to a specific content of 12.6 nmol/mg protein. The cytochrome P-450 preparation was electrophoretically homogeneous and had an apparent monomeric molecular weight of 51,000 as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The cytochrome showed catalytic activities as oxidations of N-methylaniline, ethylmorphine, N,N-dimethylaniline, N,N-dimethylnitrosamine, benzphetamine, aminopyrine, aniline, p-nitroanisole, and 7-ethoxycoumarin to various extents. In fetal liver homogenate, the amount of cytochrome P-450 that reacted with the antiserum to P-450HFLa accounted for more than 36% of the total cytochrome P-450 in three different fetal livers. On the other hand, the amount of P-450HFLa was less than 5% of the total cytochrome P-450 in adult liver microsomes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Aged
  • Cytochrome P-450 Enzyme System / immunology
  • Cytochrome P-450 Enzyme System / isolation & purification*
  • Cytochrome P-450 Enzyme System / metabolism
  • Female
  • Fetus / enzymology*
  • Humans
  • Kinetics
  • Liver / embryology
  • Liver / enzymology*
  • Male
  • Microsomes, Liver / enzymology
  • Mixed Function Oxygenases / metabolism


  • Cytochrome P-450 Enzyme System
  • Mixed Function Oxygenases