Immunoaffinity purification of aromatase cytochrome P-450 from human placental microsomes, metabolic switching from aromatization to 1β and 2β-monohydroxylation, and recognition of aromatase isozymes

This publication has 13 references indexed in Scilit:

• Rebuttal to the 1α,2β-hydrogen elimination mechanism of estrogen biosynthesis by reconstituted aromatase [Poster 03]
  Steroids, 1987
• Purification and reconstitution properties of human placental aromatase. A cytochrome P-450-type monooxygenase
  European Journal of Biochemistry, 1986
• Purification to homogeneity of aromatase from human placenta
  Biochemical and Biophysical Research Communications, 1986
• Preparation and characterization of polyclonal and monoclonal antibodies against human aromatase cytochrome P-450 (P-450AROM), and their use in its purification
  Archives of Biochemistry and Biophysics, 1985
• Estrogen synthetase. demonstration that the high molecular weight form of nadph-cytochrome c reductase from human placental microsomes is required for androgen aromatization
  The Journal of Steroid Biochemistry and Molecular Biology, 1982
• Species specificity of estrogen biosynthesis in pregnancy. Immunochemical difference of placental NADPH-cytochrome C (p-450) reductase in human, baboon and horse
  Journal of Steroid Biochemistry, 1981
• Solubilization of estrogen synthetase from human term placental microsomes using detergents
  The Journal of Steroid Biochemistry and Molecular Biology, 1978
• Estrogen biosynthesis. I. Estrogen biosynthesis. Stereospecific distribution of tritium in testosterone-1α2α-t₂
  Biochemistry, 1971
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970
• Synthesesteigerung und Abbauhemmung bei der Vermehrung der mikrosomalen Cytochrome P-450 und b-5 durch Phenobarbital
  Naunyn-Schmiedebergs Archiv für experimentelle Pathologie und Pharmakologie, 1970