Purification and reconstitution properties of human placental aromatase. A cytochrome P-450-type monooxygenase.

@article{Tan1986PurificationAR,
  title={Purification and reconstitution properties of human placental aromatase. A cytochrome P-450-type monooxygenase.},
  author={Liat Tan and Naoki Muto},
  journal={European journal of biochemistry},
  year={1986},
  volume={156 2},
  pages={
          243-50
        }
}
The hemoprotein component of human placental aromatase (estrogen synthetase) has been purified to a high degree of homogeneity by a combination of affinity and adsorption chromatography on aminohexyl-Sepharose, concanavalin-A-Sepharose, and hydroxyapatite. The monomeric form of the enzyme has an Mr of 55000 +/- 1000 as estimated by sodium dodecyl sulfate gel electrophoresis. Its absolute spectrum shows a high-spin Soret band at 394 nm while its reduced, CO-difference spectrum has a maximum at… CONTINUE READING
BETA

Citations

Publications citing this paper.
SHOWING 1-8 OF 8 CITATIONS

Aromatase inhibitors and enzyme stability.

  • Endocrine-related cancer
  • 1999
VIEW 1 EXCERPT
CITES METHODS

Similar Papers

Loading similar papers…