Purification to Homogeneity of Aromatase From Human Placenta

Biochem Biophys Res Commun. 1986 Jan 29;134(2):704-10. doi: 10.1016/s0006-291x(86)80477-6.

Abstract

Aromatase cytochrome P-450 has been purified from human placenta to homogeneity, as demonstrated by electrophoresis on polyacrylamide gels with SDS, and by double diffusion against an antibody raised in rabbits. The enzyme converts androstenedione to estrone (Vmax 13.3 n moles/min/n mole P-450; Km 30 microM) and testosterone to estradiol. Aromatase activity requires P-450, P-450 reductase and NADPH. Enzyme activity is inhibited by anti-aromatase antibodies and by 4-hydroxyandrostenedione. The enzyme shows a molecular weight of 55,000, is extremely unstable and spontaneously forms P-420 with a half-life of 2.5 days.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aromatase / isolation & purification*
  • Female
  • Humans
  • Kinetics
  • Microsomes / enzymology
  • Molecular Weight
  • Placenta / enzymology*
  • Pregnancy

Substances

  • Aromatase