Oxidative Activation of 2-aminofluorene By Human Red-blood-cell Cytosol

Duvergervanbogaert, M.;Wiame, D.;Stecca, C.
(1992) Biochemical Pharmacology — Vol. 44, n° 12, p. 2422-2424 (1992)

Files

pdfdocument.pdf
  • Restricted Access
  • Adobe PDF
  • 197.38 KB
No access

Details

Authors
  • Duvergervanbogaert, M.
    Author
  • Wiame, D.
    Author
  • Stecca, C.
    Author
Abstract
Purified red blood cell cytosol is able to activate 2-aminofluorene (2AF) to N-hydroxy-2-aminofluorene. Apparent kinetic parameters are determined with and without methylene blue. The latter, which maintains haemoglobin in the reduced form and stimulates NADPH production, the affinity of the enzyme for the 2AF. This activity is inhibited by carbon monoxide while cyanide is without effect. The involvement of a peroxidative reaction or a one-electron oxidative mechanism involving free radicals may be excluded.
Affiliations

Citations

  • APA
  • Chicago
  • FWB

Duvergervanbogaert, M., Wiame, D., & Stecca, C. (1992). Oxidative Activation of 2-aminofluorene By Human Red-blood-cell Cytosol. Biochemical Pharmacology, 44(12), 2422-2424. https://doi.org/10.1016/0006-2952(92)90691-B (Original work published 1992)